The extinction of the Dinosaur was a tumultuous time that included some of the largest volcanic eruptions in Earth’s history, as well as the impact of a 10-15 km wide asteroid. The role these events played in the extinction of the dinosaurs has been fiercely debated over the past several decades.

New findings, published today in the journal , suggest that while massive volcanic eruptions in India contributed to Earth’s climate changes, they may not have played the major role in the extinction of dinosaurs, and the asteroid impact was the primary driver of the end-Cretaceous mass extinction.

By analysing ancient peats from Colorado and North Dakota in the USA, the researchers – led by The University of Manchester – reconstructed the average annual air temperatures in the 100,000 years leading up to the extinction.

The scientists, including from the University of Plymouth, Utrecht University in the Netherlands, and Denver Museum of Nature and Science in the USA, found that volcanic CO₂ emissions caused a slow warming of about 3°C across this period. There was also a short cold “snap” — cooling of about 5°C — that coincided with a major volcanic eruption 30,000 years before the extinction event that was likely due to volcanic sulphur emissions blocking-out sunlight.

However, temperatures returned to stable pre-cooling temperatures around 20,000 years before the mass extinction of dinosaurs, suggesting the climate disruptions from the volcanic eruptions weren’t catastrophic enough to kill them off dinosaurs.

Dr Lauren O’Connor, lead scientist and now Research Fellow at Utrecht University, said: “These volcanic eruptions and associated CO₂ emissions drove warming across the globe and the sulphur would have had drastic consequences for life on earth. But these events happened millennia before the extinction of the dinosaurs, and probably played only a small part in the extinction of dinosaurs.”

The fossil peats that the researchers analysed contain specialised cell-membrane molecules produced by bacteria. The structure of these molecules changes depending on the temperature of their environment. By analysing the composition of these molecules preserved in ancient sediments, scientists can estimate past temperatures and were able to create a detailed "temperature timeline" for the years leading up to the dinosaur extinction.

Dr Tyler Lyson, scientist at the Denver Museum of Nature and Science, said: “The field areas are ~750 km apart and both show nearly the same temperature trends, implying a global rather than local temperature signal. The trends match other temperature records from the same time period, further suggesting that the temperature patterns observed reflect broader global climate shifts.”

Bart van Dongen, Professor of Organic Geochemistry at The University of Manchester, added: “This research helps us to understand how our planet responds to major disruptions. The study provides vital insights not only into the past but could also help us find ways for how we might prepare for future climate changes or natural disasters.”

The team is now applying the same approach to reconstruct past climate at other critical periods in Earth’s history.

A group of leading international scientists is calling for a global conversation about the potential creation of "mirror bacteria"—a hypothetical form of life built with biological molecules that are the opposite of those found in nature.

In a new report published today in the journal , the researchers, including Professor Patrick Cai, a world leader in synthetic genomics and biosecurity, from The University of Manchester, explain that these mirrored organisms would differ fundamentally from all known life and could pose risks to ecosystems and human health if not carefully managed.

Driven by scientific curiosity, some researchers around the world are beginning to explore the possibility of creating mirror bacteria, and although the capability to engineer such life forms is likely decades away and would require major technological breakthroughs, the researchers are calling for a broad discussion among the global research community, policymakers, research funders, industry, civil society, and the public now to ensure a safe path forward.

Professor Cai said: “While mirror bacteria are still a theoretical concept and something that we likely won’t see for a few decades, we have an opportunity here to consider and pre-empt risks before they arise.

“These bacteria could potentially evade immune defences, resist natural predators, and disrupt ecosystems. By raising awareness now, we hope to guide research in a way that prioritises safety for people, animals, and the environment."

The analysis is conducted by 38 scientists from nine countries including leading experts in immunology, plant pathology, ecology, evolutionary biology, biosecurity, and planetary sciences. The publication in is accompanied by a detailed 300-page .

The analysis concluded that mirror bacteria could broadly evade many immune defences of humans, animals, and potentially plants.

It also suggests that mirror bacteria could evade natural predators like viruses and microbes, which typically control bacterial populations. If they were to spread, these bacteria could move between different ecosystems and put humans, animals, and plants at continuous risk of infection.

The scientists emphasise that while speculative, these possibilities merit careful consideration to ensure scientific progress aligns with public safety.

Professor Cai added: “At this stage, it’s also important to clarify that some related technologies, such as mirror-image DNA and proteins, hold immense potential for advancing science and medicine. Similarly, synthetic cell research, which does not directly lead to mirror bacteria, is critical to advancing basic science. We do not recommend restricting any of these areas of research. I hope this is the starter of many discussions engaging broader communities and stakeholders soon. We look forward to hosting a forum here in 91ֱ�� in autumn 2025.”

Going forward, the researchers plan to host a series of events to scrutinise their findings and encourage open discussion about the report. For now, they recommend halting any efforts toward the creation of mirror bacteria and urge funding bodies not to support such work. They also propose examining the governance of enabling technologies to ensure they are managed responsibly.

, which aims to improve the way prosthetics for people who have suffered traumatic limb loss work, wowed the judges at the (iGEM) 2024 Grand Jamboree.

The non-profit iGEM Foundation hosts an international student competition each year to promote education and collaboration among new generations of synthetic biologists.

Human-machine interfaces are becoming more advanced, with new technologies harnessing the body’s electric signals to control devices.

Artificial limbs, known as myoelectric prosthetics, are directed by electrical signals generated by muscle contractions in the residual limb, which can be translated to motion.

However, heavy batteries and motors in myoelectric prosthetics can cause excessive sweating and make the electrodes slip from their contact points, resulting in discomfort and imprecise limb movement.

To solve the problem, the team proposed using synthetic biology to create tiny specially designed wires that work with skin cells.

They engineered a type of bacteria – Escherichia coli – to express tiny, hair-like structures known as pili (e-pili) found on electricity conducting bacteria called Geobacter sulfurreducens.

By combining the Escherichia coli with a protein-binding peptide, the team created nanowires that specifically target and bind to proteins at the skin’s surface, potentially enhancing the precision of an artificial limb.

The 91ֱ�� iGEM team were Damian Ungureanu, Devika Shenoy, Francisco Correia, Janet Xu, Jia Run Dong, Usrat Nubah, Yuliia Anisimova, and Zainab Atique-Ur-Rehman.

, said: “I’m delighted our team won gold at the iGEM 2024 Grand Jamboree for an innovation which could make a difference for people who need artificial limbs.

She added: “I have supervised the 91ֱ�� iGEM teams together with Professor Rainer Breitling since 2013.

“Our teams, based in the (MIB), have been very successful and have achieved a gold medal all but one of the years that we participated - which is quite an achievement.

“In 2016, the team also scooped the special award for ‘Best Computational Model’ and were shortlisted for the ‘Best Education and Public Engagement’ award.”

This year’s 91ֱ�� iGEM team worked in the MIB labs throughout the summer, with financial and logistical support from the MIB, School of Biological Sciences, School of Social Sciences/Department of Social Anthropology, School of Arts Languages and Cultures, and the Future Biomanufacturing Research Hub.

The team also worked with the (AMBS) to comprehensively explore the social and economic implications of their ideas using a (RRI) approach.

The competition provides an interdisciplinary learning opportunity for students outside biology, by encouraging participants to think beyond their lab work.

Damian Ungureanu, second year Biochemistry student, said: “Working with people from different cultural and academic backgrounds has allowed me to substantially develop my communication skills. Even though this was a synthetic biology project, the human practices aspect was just as important as the science. Winning the gold medal felt like the culmination of one year of hard work.”

Devika Shenoy, second year Biomedical Sciences student, said: “I am grateful to have gotten the opportunity to work with so many like-minded individuals and under the guidance of skilled advisors and PIs. iGEM has truly broadened my horizons and understanding of how science and synthetic biology can be used to solve world issues.”

Biocatalysis is a process that uses enzymes as natural catalysts to carry out chemical reactions. Scientists at The University of Manchester and AstraZeneca have developed a new biocatalytic pathway that uses enzymes to produce nucleoside analogues, which are vital components in many pharmaceuticals used to treat conditions like cancer and viral infections.

Typically, producing these analogues is complicated, time consuming and generates significant waste. However, in a new breakthrough, published in the journal , the researchers have demonstrated how a "biocatalytic cascade" — a sequence of enzyme-driven reactions — can simplify the process, potentially cutting down production time and reducing environmental impact.

The researchers engineered an enzyme called deoxyribose-5-phosphate aldolase, enhancing its range of functions to efficiently produce different sugar-based compounds, which serve as building blocks for nucleoside-based medicines, such as oligonucleotide therapeutics. These building blocks were combined using additional enzymes to develop a condensed protocol for the synthesis of nucleoside analogues which simplifies the traditional multi-step process to just two or three stages, significantly improving efficiency.

With further refinement, this method could help streamline the production of a wide range of medicines, while significantly reducing their environmental footprint. The team are now continuing this work with the MRC funded , which looks to develop sustainable biocatalytic routes towards functionalised nucleosides, nucleotides and oligonucleotides.

The study, led by scientists at The University of Manchester, has revealed that a material known as a metal-organic framework (MOF) - an ultra-porous material - can be modified to capture and filter out significantly more benzene from the atmosphere than current materials in use.

Benzene is primarily used as an industrial solvent and in the production of various chemicals, plastics, and synthetic fibres, but can also be released into the atmosphere through petrol stations, exhaust fumes and cigarette smoke. Despite its widespread applications, benzene is classified as a human carcinogen, and exposure can lead to serious health effects, making careful management and regulation essential.

The research, published in the journal today, could lead to significant improvements in air quality both indoors and outdoors.

MOFs are advanced materials that combine metal centres and organic molecules to create porous structures. They have a highly adjustable internal structure, making them particularly promising for filtering out harmful gases from the air.

The researchers modified the MOF structure – known as MIL-125 – by incorporating single atoms from different elements, including zinc, iron, cobalt, nickel and copper to test which would most effectively capture benzene.

They discovered that adding a single zinc atom to the structure significantly enhanced the material’s efficiency, enabling it to capture benzene even at ultra-low concentrations – measured at parts per million (ppm) – a significant improvement over current materials.

The new material – now known as MIL-125-Zn – demonstrates a benzene uptake of 7.63 mmol per gram of material, which is significantly higher than previously reported materials.

It is also highly stable even when exposed to moisture, maintaining its ability to filter benzene for long periods without losing effectiveness. Tests show that it can continue removing benzene from air even under humid conditions.

As the research progresses, the team will look to collaborate with industry partners to develop this and related new materials, with the potential of integrating it into ready-made devices, such as air purification systems in homes, workplaces, and industrial settings.

These findings have the potential to accelerate the discovery of novel, more efficient cryoprotectants - and may also allow for the repurposing of molecules already known to slow or stop ice growth.

Professor Matthew Gibson, from 91ֱ�� Institute of Biotechnology at The University of Manchester, added: “My team has spent more than a decade studying how ice-binding proteins, found in polar fish, can interact with ice crystals, and we’ve been developing new molecules and materials that mimic their activity. This has been a slow process, but collaborating with Professor Sosso has revolutionized our approach. The results of the computer model were astonishing, identifying active molecules I never would have chosen, even with my years of expertise. This truly demonstrates the power of machine learning.”

The full paper can be read .

Sugars play a crucial role in human health and disease, far beyond being just an energy source. Complex sugars called glycans coat all our cells and are essential for healthy function. However, these sugars are often hijacked by pathogens such as influenza, Covid-19, and cholera to infect us.

One big problem in treating and diagnosing diseases and infections is that the same glycan can bind to many different proteins, making it hard to understand exactly what’s happening in the body and has made it difficult to develop precise medical tests and treatments.

In a breakthrough, published in the journal , a collaboration of academic and industry experts in Europe, including from The University of Manchester and the University of Leeds, have found a way to create unnatural sugars that could block the pathogens.

The finding offers a promising avenue to new drugs and could also open doors in diagnostics by ‘capturing’ the pathogens or their toxins.

, a researcher from at The University of Manchester, said “During the Covid-19 pandemic, our team introduced the first lateral flow tests which used sugars instead of antibodies as the ‘recognition unit’. But the limit is always how specific and selective these are due to the promiscuity of natural sugars. We can now integrate these fluoro-sugars into our biosensing platforms with the aim of having cheap, rapid, and thermally stable diagnostics suitable for low resource environments.”

Professor Bruce Turnbull, a lead author of the paper from the School of Chemistry and Astbury Centre for Structural Molecular Biology at The University of Leeds, said “Glycans that are really important for our immune systems, and other biological processes that keep us healthy, are also exploited by viruses and toxins to get into our cells. Our work is allowing us to understand how proteins from humans and pathogens have different ways of interacting with the same glycan. This will help us make diagnostics and drugs that can distinguish between human and pathogen proteins.”

The researchers used a combination of enzymes and chemical synthesis to edit the structure of 150 sugars by adding fluorine atoms. Fluorine is very small meaning that the sugars keep their same 3D shape, but the fluorines interfere with how proteins bind them.

, a researcher from 91ֱ�� Institute of Biotechnology at The University of Manchester, said “One of the key technologies used in this work is biocatalysis, which uses enzymes to produce the very complex and diverse sugars needed for the library. Biocatalysis dramatically speeds up the synthetic effort required and is a much more green and sustainable method for producing the fluorinated probes that are required.”

They found that some of the sugars they prepared could be used to detect the cholera toxin – a harmful protein produced by bacteria – meaning they could be used in simple, low-cost tests, similar to lateral flow tests, widely used for pregnancy testing and during the COVID-19 pandemic.

Dr Kristian Hollie, who led production of the fluoro-sugar library at the University of Leeds, said: “We used enzymes to rapidly assemble fluoro-sugar building blocks to make 150 different versions of a biologically important glycan. We were surprised to find how well natural enzymes work with these chemically modified sugars, which makes it a really effective strategy for discovering molecules that can bind selectively.”

The study provides evidence that the artificial “fluoro-sugars” can be used to fine-tune pathogen or biomarker recognition or even to discover new drugs. They also offer an alternative to antibodies in low-cost diagnostics, which do not require animal tests to discover and are heat stable.

The research team included researchers from eight different universities, including 91ֱ��, Imperial College London, Leeds, Warwick, Southampton, York, Bristol, and Ghent University in Belgium.

The breakthrough, published in the journal , could significantly improve accessibility of essential protein-based drugs in developing countries where cold storage infrastructure may be lacking, helping efforts to diagnose and treat more people with serious health conditions.

The researchers, from the Universities of Manchester, Glasgow and Warwick, have designed a hydrogel – a material mostly made of water – that stabilises proteins, protecting its properties and functionality at temperatures as high as 50°C.

The technology keeps proteins so stable that they can even be sent through the post with no loss of effectiveness, opening up new possibilities for more affordable, less energy-intensive methods of keeping patients and clinics supplied with vital treatments.

Protein therapeutics are used to treat a range of conditions, from cancer to diabetes and most recently to treat obesity and play a vital role in modern medicine and biotechnology. However, keeping them stable and safe for storage and transportation is a challenge. They must be kept cold to prevent any deterioration, using significant amounts of energy and limiting equitable distribution in developing countries.

The medicines also often include additives – called excipients – which must be safe for the drug and its recipients limiting material options.

The findings could have major implications for the diagnostics and pharmaceutical industries.

, is one of the paper’s corresponding authors. He said: “In the early days of the Covid vaccine rollout, there was a lot of attention given in the news media to the challenges of transporting and storing the vaccines, and how medical staff had to race to put them in people’s arms quickly after thawing.  

“The technology we’ve developed marks a significant advance in overcoming the challenges of the existing ‘cold chain’ which delivers therapeutic proteins to patients. The results of our tests have very encouraging results, going far beyond current hydrogel storage techniques’ abilities to withstand heat and vibration. That could help create much more robust delivery systems in the future, which require much less careful handling and temperature management.”

The hydrogel is built from a material called a low molecular weight gelator (LMWG), which forms a three-dimensional network of long, stiff fibres. When proteins are added to the hydrogel, they become trapped in the spaces between the fibres, where they are unable to mix and aggregate – the process which limits or prevents their effectiveness as medicines.

The unique mechanical properties of the gel’s network of fibres, which are stiff but also brittle, ensures the easy release of a pure protein. When the protein-storing gel is stored in an ordinary syringe fitted with a special filter, pushing down on the plunger provides enough pressure to break the network of fibres, releasing the protein. The protein then passes cleanly through the filter and out the tip of the syringe alongside a buffer material, leaving the gel behind.

In the paper, the researchers show how the hydrogel works to store two valuable proteins: insulin, used to treat diabetes, and beta-galactosidase, an enzyme with numerous applications in biotechnology and life sciences.

Ordinarily, insulin must be kept cold and still, as heating or shaking can prevent it from being an effective treatment. The team tested the effectiveness of their hydrogel suspension for insulin by warming samples to 25°C and rotating them at 600 revolutions per minute, a strain test far beyond any real-world scenario. Once the tests were complete, the team were able to recover the entire volume of insulin from the hydrogel, showing that it had been protected from its rough treatment.

The team then tested samples of beta-galactosidase in the hydrogel, which was stored at a temperature of 50°C for seven days, a level of heat exceeding any realistic temperature for real-world transport. Once the enzyme was extracted from the hydrogel, the team found it retained 97% of its function compared against a fresh sample stored at normal temperature.

A third test saw the team put samples of proteins suspended in hydrogel into the post, where they spent two days in transit between locations. Once the sample arrived at its destination, the team’s analysis showed that the gels’ structures remained intact and the proteins had been entirely prevented from aggregating.

is the paper’s other corresponding author. He said: “Delivering and storing proteins intact is crucial for many areas of biotechnology, diagnostics and therapies. Recently, it has emerged that hydrogels can be used to prevent protein aggregation, which allows them to be kept at room temperature, or warmer. However, separating the hydrogel components from the protein or proving that they are safe to consume is not always easy. Our breakthrough eliminates this barrier and allows us to store and distribute proteins at room temperature, free from any additives, which is a really exciting prospect.”

The team are now exploring commercial opportunities for this patent-pending technology as well as further demonstrating its applicability. 

Researchers from the University of East Anglia and Diamond Light Source Ltd also contributed to the research. The team’s paper, titled ‘Mechanical release of homogenous proteins from supramolecular gels’, is published in Nature.

The research was supported by funding from the European Union’s Horizon 2020 programme, the European Research Council, the Royal Society, the Engineering and Physical Sciences Research Council (EPSRC), the University of Glasgow and UK Research and Innovation (UKRI).

Peptides are comprised of small chains of amino acids, which are also the building blocks of proteins. Peptides play a crucial role in our bodies and are used in many medicines to fight diseases such as cancer, diabetes, and infections. They are also used as vaccines, nanomaterials and in many other applications. However, making peptides in the lab is currently a complicated process involving chemical synthesis, which produces a lot of harmful waste that is damaging to the environment.

In a new breakthrough, published in the journal , 91ֱ�� scientists have discovered a new family of ligase enzymes – a type of molecular glue that can help assemble short peptide sequences more simply and robustly, yielding significantly higher quantities of peptides compared to conventional methods.

The breakthrough could revolutionise the production of treatments for cancer and other serious illnesses, offering a more effective and environmentally friendly method of production.

For many years, scientists have been working on new ways to produce peptides. Most existing techniques rely on complex and heavily protected amino acid precursors, toxic chemical reagents, and harmful volatile organic solvents, generating large amounts of hazardous waste. The current methods also incur high costs, and are difficult to scale up, resulting in limited and expensive supplies of important peptide medicines.

The team in 91ֱ�� searched for new ligase enzymes involved in the biological processes that assemble natural peptides in simple bacteria. They successfully isolated and characterised these ligases and tested them in reactions with a wide range of amino acid precursors. By analysing the sequences of the bacterial ligase enzymes, the team identified many other clusters of ligases likely involved in other peptide pathways.

The study provides a blueprint for how peptides, including important medicines, can be made in the future.

, who also worked on the project said, “The ligases we discovered provide a very clean and efficient way to produce peptides. By searching through available genome sequence data, we have found many types of related ligase enzymes. We are confident that using these ligases we will be able to assemble longer peptides for a range of other therapeutic applications.”

Following the discovery, the team will now optimise the new ligase enzymes, to improve their output for larger scale peptide synthesis. They have also established collaborations with a number of the top pharmaceutical companies to help with rolling out the new ligase enzyme technologies for manufacturing future peptide therapeutics.

Dr Selena Lockyer, Professor Matthew Gibson, Professor Sarah Lovelock and the Functional Framework Materials: Design and Characterisation Team, led by and Professor Sihai Yang have all been recognised with a prize this year.

Dr Selena Lockyer has been named winner of the Royal Society of Chemistry’s Dalton Emerging Researcher Prize for her synthetic and spectroscopic studies of molecular magnets, particularly supramolecular assemblies that could be used in quantum information processing. Dr Lockyer will also receive £3000 and a medal.

Dr Lockyer investigates the properties of individual electrons at the molecular level and how they can interact with one another and relay or store information. This is done at the National Service for Electron Paramagnetic Resonance Spectroscopy at The University of Manchester.

Apart from making devices smaller, quantum devices possess other advantages. One such phenomenon is known as a superposition state that can be used in quantum bits (qubits), which a standard classical bit – the ones in our laptops – is unable to achieve.

A quantum computer will help us address society's challenges by modelling and developing solutions for climate change, sustainability and energy sources, medical conditions, and how to make a more efficient and better quantum computer.

After receiving the prize, Dr Lockyer said: “It’s such an honour and privilege to receive this award. Unexpected, as there are so many up-and-coming scientists working on numerous research areas, which makes this all the more special. When you look back at the list of previous winners, it is overwhelming to now be part of this.”

has been named winner of the Royal Society of Chemistry’s Corday-Morgan Prize.

Professor Gibson won the prize for transformative contributions in polymer and biomaterials science, particularly for the development of materials to stabilise biologics. Professor Gibson will also receive £5000 and a medal.

Storing and transporting biological materials is crucial to modern life, from frozen food to the safe delivery of blood transfusions, stem cells, or even organs. Professor Gibson and his team have learned from some of nature’s toughest organisms, which can survive sub-zero temperatures, to develop new materials which can protect biopharmaceuticals against cold stress.

After receiving the prize, Professor Gibson said: “I’m honoured to be recognised for the work we have done in my team to develop new tools to help us stabilize biologics against cold stress and to join a such a distinguished list of former awardees.”

has been named winner of the Royal Society of Chemistry’s Harrison-Meldola Prize.

Dr Lovelock won the prize for the development of innovative biocatalytic approaches to produce therapeutic oligonucleotides. She also receives £5000 and a medal.

Therapeutic oligonucleotides are a new class of RNA-based molecules that have the potential to treat a wide range of diseases. However, the rapidly growing number of therapies approved and in advanced clinical trials is placing unprecedented demands on our capacity to manufacture oligonucleotides at scale.

Biocatalysis is an exciting technology that is widely used across the chemical industry: this is where enzymes are used to convert starting materials into high-value products. Dr Lovelock’s group is developing biocatalytic approaches to produce therapeutic oligonucleotides in a more sustainable and scalable way.

One strategy they have developed produces complex oligonucleotide sequences in a single operation using polymerases and endonucleases (nature’s enzymes). These enzymes work together to amplify complementary sequences embedded within a catalytic template. The group is working in partnership with industry to translate their approaches into manufacturing processes.

After receiving the prize, Dr Lovelock said: “I am delighted to have been awarded the 2024 Harrison-Meldola Memorial Prize. I am very grateful to my talented research group. It is their hard work, great ideas, and dedication that has made this award possible.”

The Functional Framework Materials: Design and Characterisation Team have been named winners of the Royal Society of Chemistry’s Horizon Prize, which celebrates discoveries and innovations that push the boundaries of science.

The team is a collaboration between The University of Manchester, Oak Ridge National Laboratory, Diamond Light Source, ISIS Neutron and Muon Source STFC, Berkeley Advanced Light Source, Peking University, Xiamen University and the University of Chicago.

They were awarded the prize for seminal contributions to in situ and operando characterisation of porous materials and catalysts for the binding, capture and separation of fuels, hydrocarbons, and pollutants. The team receive a trophy and a video showcasing their work, and each team member receives a certificate.

Metal-organic frameworks (MOFs) are porous materials that can capture and store important fuels like hydrogen, methane, and ammonia, hydrocarbons (ethane, propane, and xylenes), and harmful pollutants (carbon dioxide, sulfur dioxide, and nitrogen dioxide).

Using state-of-the-art X-ray and neutron techniques, the team have been able to see the MOFs at the atomic level and how the captured molecules interact with the MOF’s internal structure during reactions. They also used computational modelling to give a deep understanding of how these advanced functional materials operate at a molecular level. This extensive collaboration has been crucial for producing improved materials that can be integrated into our daily lives and makes a vital contribution towards solving the pressing climate and energy challenges that the world faces.

Professor Martin Schröder, Vice President and Dean, Faculty of Science and Engineering, who leads the group at The University of Manchester, said: “I am delighted and honoured that the Royal Society of Chemistry has recognised our interdisciplinary team with the Dalton Horizon Prize. This has been a truly international collaborative effort spanning multiple individuals and groups each bringing their own unique expertise to address challenge research areas.”

The Royal Society of Chemistry’s prizes have recognised excellence in the chemical sciences for more than 150 years. This year’s winners join a prestigious list of past winners in the RSC’s prize portfolio, 60 of whom have gone on to win Nobel Prizes for their work, including 2022 Nobel laureate Carolyn Bertozzi and 2019 Nobel laureate John B Goodenough.

The Research and Innovation Prizes celebrate brilliant individuals across industry and academia. They include prizes for those at different career stages in general chemistry and for those working in specific fields, as well as interdisciplinary prizes and prizes for those in specific roles. The Horizon Prizes highlight exciting, contemporary chemical science at the cutting edge of research and innovation. These prizes are for groups, teams and collaborations of any form or size who are opening up new directions and possibilities in their field, through groundbreaking scientific developments. Other prize categories include those for Education (announced in November), the Inclusion & Diversity Prize, and Volunteer Recognition Prizes.

Dr Helen Pain, Chief Executive of the Royal Society of Chemistry, said: “The chemical sciences cover a rich and diverse collection of disciplines, from fundamental understanding of materials and the living world to applications in medicine, sustainability, technology and more. By working together across borders and disciplines, chemists are finding solutions to some of the world’s most pressing challenges.

“Our prize winners come from a vast array of backgrounds, all contributing in different ways to our knowledge-base and bringing fresh ideas and innovations. We recognise chemical scientists from every career stage and every role type, including those who contribute to the RSC’s work as volunteers. We celebrate winners from both industry and academia, as well as individuals, teams, and the science itself.

“Their passion, dedication and brilliance are an inspiration. I extend my warmest congratulations to them all.”

For more information about the RSC’s prizes portfolio, visit .

The centre has been awarded £1.2m through an International Centre to Centre grant from the Engineering and Physical Sciences Research Council, part of UK Research and Innovation. Led by Professor , Interim Director of the MIB, along with Professor and Dr , and in partnership with Professor David Baker from the Institute of Protein Design (IPD) at the University of Washington, ICED will employ the latest deep-learning protein design tools to accelerate the development of new biocatalysts for use across the chemical industry. The centre will deliver customised biocatalysts for sustainable production of a wide range of chemicals and biologics, including pharmaceuticals, agrochemicals, materials, commodity chemicals and advanced synthetic fuels.

Biocatalysis uses natural or engineered enzymes to speed up valuable chemical processes. This technology is now widely recognised as a key enabling technology for developing a greener and more efficient chemical industry. Although powerful, existing experimental methods for developing industrial biocatalysts are costly and time-consuming, and this restricts the potential impact of biocatalysis on many industrial processes. Furthermore, for many desirable chemical transformations there are no known enzymes that can serve as starting templates for experimental engineering. In ICED we will bring together leading computational and experimental teams from across academia and industry to bring about a step-change in the speed of biocatalyst development. The approaches developed will also allow the development of new families of enzymes with catalytic functions that are unknown in nature.

Professor David Baker, lead researcher from the Institute of Protein Design says; “Accurately designing efficient enzymes with new catalytic functions is one of the grand challenges for the protein design field. We are thrilled to be working with Professor Green and his team in the MIB to address this crucial biotechnological challenge.’’

The design tools developed throughout the project will be readily available to specialists and non-specialists to support their own enzyme engineering and biocatalysis needs. As the centre develops, we expect to grow our partnerships with the wider academic and industrial sector to ensure that we can best serve the needs and ambitions of the global biocatalysis community.

With the chemical and pharmaceutical industries contributing £30.7bn to the UK economy alone, technologies like biocatalysis are poised to revolutionise how every day, essential products are made while also benefitting our health and our environment.

Beth Sims, a third-year Chemistry student at The University of Manchester, will join a group of 18 students, all on work placement at , a science company in Derbyshire, to take part in the challenge to raise money for , an important charity supporting students with their mental health.

The Lubrizol students will be completing the distance between Lubrizol in Hazelwood, Derbyshire, and the company’s base in Barcelona. They are aiming to cover the 1715km (1066 miles) distance collectively, with each student taking on roughly 100km during April, whether that be walking, running, cycling, or even climbing. 

Beth enjoys going for jogs in Lubrizol’s extensive grounds, which are set in the beautiful Derbyshire countryside in a former stately home near Duffield and will be running the distance throughout the challenge.

With around one in four students reporting having a diagnosed mental health issue while at university, Student Minds empowers students to build their own mental health toolkit to support themselves and their peers through university life and beyond. The students are aiming to raise £500 with their distance challenge, which will be matched by Lubrizol. To donate, visit:

Other universities represented by the Lubrizol distance challenge are: Derby, Loughborough, York, Warwick, Nottingham, Lincoln, Durham, St Andrews and Sheffield.

describe a force-controlled release system that harnesses natural forces to trigger targeted release of molecules, which could significantly advance medical treatment and smart materials.

The discovery, published today in the journal , uses a novel technique using a type of interlocked molecule known as rotaxane. Under the influence of mechanical force - such as that observed at an injured or damaged site - this component triggers the release of functional molecules, like medicines or healing agents, to precisely target the area in need. For example, the site of a tumour.

It also holds promise for self-healing materials that can repair themselves in situ when damaged, prolonging the lifespan of these materials. For example, a scratch on a phone screen.

Traditionally, the controlled release of molecules with force has presented challenges in releasing more than one molecule at once, usually operating through a molecular "tug of war" game where two polymers pull at either side to release a single molecule.

The new approach involves two polymer chains attached to a central ring-like structure that slide along an axle supporting the cargo, effectively releasing multiple cargo molecules in response to force application. The scientists demonstrated the release of up to five molecules simultaneously with the possibility of releasing more, overcoming previous limitations.

The breakthrough marks the first time scientists have been able to demonstrate the ability to release more than one component, making it one of the most efficient release systems to date.

The researchers also show versatility of the model by using different types of molecules, including drug compounds, fluorescent markers, catalyst and monomers, revealing the potential for a wealth of future applications.

Looking ahead, the researchers aim to delve deeper into self-healing applications, exploring whether two different types of molecules can be released at the same time. For example, the integration of monomers and catalysts could enable polymerization at the site of damage, creating an integrated self-healing system within materials.

They will also look to expand the sort of molecules that can be released.

said: "We've barely scratched the surface of what this technology can achieve. The possibilities are limitless, and we're excited to explore further."

They have developed a new catalyst which has been shown to have a wide variety of uses and the potential to streamline optimisation processes in industry and support new scientific discoveries.

Catalysts, often considered the unsung heroes of chemistry, are instrumental in accelerating chemical reactions, and play a crucial role in the creation of most manufactured products. For example, the production of polyethylene, a common plastic used in various everyday items such as bottles and containers or found in cars to convert harmful gases from the engine's exhaust into less harmful substances.

Among these, ruthenium – a platinum group metal – has emerged as an important and commonly used catalyst. However, while a powerful and cost-effective material, highly reactive ruthenium catalysts have long been hindered by their sensitivity to air, posing significant challenges in their application. This means their use has so far been confined to highly trained experts with specialised equipment, limiting the full adoption of ruthenium catalysis across industries.

In new research published in the journal Nature Chemistry, scientists at The University of Manchester working with collaborators at global biopharmaceutical company AstraZeneca unveil a ruthenium catalyst proven to be long-term stable in air while maintaining the high reactivity necessary to facilitate transformative chemical processes.

The discovery allows for simple handling and implementation processes and has shown versatility across a wide array of chemical transformations, making it accessible for non-specialist users to exploit ruthenium catalysis. Collaborative efforts with AstraZeneca demonstrate this new catalyst’s applicability to industry, particularly in developing efficient and sustainable drug discovery and manufacturing processes.

Dr James Douglas, Director of High-Throughput Experimentation who collaborated on the project from AstraZeneca said: “Catalysis is a critical technology for AstraZeneca and the wider biopharmaceutical industry, especially as we look to develop and manufacture the next generation of medicines in a sustainable way. This new catalyst is a great addition to the toolbox and we are beginning to explore and understand its industrial applications.”

The new approach has already led to the discovery of new reactions that have never been reported with ruthenium and with its enhanced versatility and accessibility, the researchers anticipate further advancements and innovations in the field.

McArthur, G., Docherty, J.H., Hareram, M.D. et al. An air- and moisture-stable ruthenium precatalyst for diverse reactivity. Nat. Chem. (2024). https://doi.org/10.1038/s41557-024-01481-5

The bid was delivered by a coordination team, which includes and from the University and has secured £49.35m from the UKRI Infrastructure Fund to establish C-MASS - a national hub-and-spoke infrastructure designed to integrate and advance the country’s capability in mass spectrometry.

Mass spectrometry is a central analytical technique that quantifies and identifies molecules by measuring their mass and charge. It is used across science and medicine, for drug discovery, to screen all newborn babies for the presence of metabolic disorders, to monitor pollution and to tell us what compounds are in the tails of comets.

Researchers at The University of Manchester develop and apply mass spectrometry in many of its research centres and institutes, including the , the , , , the , and the

C-MASS will enable rapid methodological advances, by developing consensus protocols to allow population level screening of health markers and accelerated data access and sharing. It will bring together cutting-edge instrumentation at a range of laboratories connected by a coordinating central hub that will manage a central metadata catalogue. Together, this will provide unparalleled signposting of data and will be a critical measurement science resource for the UK.

The bid for the funding has been developed over the last 10 years and has included input and support from more than 40 higher education institutes, 35 industrial partners and numerous research institutes.

91ֱ�� is renowned for its expertise in mass spectrometry. J.J. Thomson, who was an alumnus of The University of Manchester, built the first mass spectrometer - originally called a parabola spectrograph - in 1912. Later, another alumnus, James Chadwick, commissioned the first commercial mass spectrometer, built by the 91ֱ�� firm Metropolitan Vickers, for use in the second world war to separate radioactive isotopes.

Now, many decades later, the University receives more funding in mass spectrometry than any other higher education institution in the UK and more mass spectrometers are made in the 91ֱ�� region than any other in Europe.

At the University, researchers across a range of disciplines including , , use mass spectrometry for wide range of world-leading research. Just some of those projects include: , improving the testing and diagnosis of womb cancer, improving our understanding of Huntington’s disease and rheumatic heart disease, diagnosing Parkinson’s disease and finding treatments for blindness.

The mass spectrometry laboratories at the University boast a range of industry-leading instrumentations, not just for staff and students, but also collaborating with many external companies. 

91ֱ�� is the recipient of five awards, including:

• , Senior Lecturer in Chemical Biology and Biological Chemistry of the , and , Professor of Polymer Science at the Henry Royce Institute, who are a Co-Investigators on a Mission Hub led by the University of Portsmouth. The mission Hub is looking into how engineering biology can tackle plastic waste.
• , Professor of Geomicrobiology, from the Department of Earth and Environmental Sciences, is involved in a Mission Hub led by the University of Kent, and also leads a Mission Award, both of which will be looking at ways to use engineering biology to process metals, including for bioremediation and for metal recovery from industrial waste streams.
• , , and of the 91ֱ�� Institute of Biotechnology, received a Mission Award for a project that will engineer biological systems to enable economical production of functionalised proteins including biopharmaceuticals and industrial biocatalysts.
• , Chair in Evolutionary Biology, from the Division of Evolution, Infection and Genomics, and Professor Patrick Cai of the 91ֱ�� Institute of Biotechnology, are looking into engineering phages with intrinsic biocontainment to develop new treatments against drug-resistant bacterial infections.

The hubs are funded for five years through UKRI and the Biotechnology and Biological Sciences Research Council (BBSRC) and are a collaboration between academic institutions and industrial partners. The Mission Award Projects are funded for two years. These projects will expand upon our current knowledge of engineering biology and capitalise on emerging opportunities.

Announcing the funding the Science, Research and Innovation Minister, Andrew Griffith, said: “Engineering biology has the power to transform our health and environment, from developing life-saving medicines to protecting our environment and food supply and beyond.

“Our latest £100m investment through the UKRI Technology Missions Fund will unlock projects as diverse as developing vaccines…preventing food waste through disease resistant crops, reducing plastic pollution, and even driving efforts to treat snakebites.

“With new Hubs and Mission Awards spread across the country, from Edinburgh to Portsmouth, we are supporting ambitious researchers and innovators around the UK in pioneering groundbreaking new solutions which can transform how we live our lives, while growing our economy.”

Engineering biology has the potential to tackle a diverse range of global challenges, driving economic growth in the UK and around the world, as well as increase national security, resilience and preparedness.  The University of Manchester has a broad range of expertise in engineering biology across its three Faculties and is also home to the international centre of excellence, the 91ֱ�� Institute of Biotechnology.

In Dr Stefan Hoffmann, lead author on the paper, and have found that by adding an estradiol-controlled destabilising domain degron (ERdd) to the genetic makeup of baker's yeast (Saccharomyces cerevisiae), they can control survival of the organism.

Destabilising domain (DD) degrons are an element of a protein that allow for degradation, unless a particular ligand – a small molecule that binds with the DD degron – is present to stabilise it. The researchers engineered the yeast to degrade proteins essential for life unless estradiol, a type of oestrogen, was present. Without estradiol, the yeast would die.

This new genetic containment technique differs from previous techniques in that it directly targets essential proteins. It has no detrimental effects on organism function, even when compared with the wild-type organism and it remains an active part of the genome, even after 100 generations.

To achieve this, the researchers tagged 775 essential genes with the ERdd tag and screened the resulting organisms for estradiol-dependent growth. Through this screening, they identified three genes, SPC110, DIS3, and RRP46 as suitable targets. The modified yeast grew well in the presence of estradiol and failed to thrive in its absence.

Professor Patrick Cai, Chair in Synthetic Genomics, said: “Safety mechanisms are instrumental for the deployment of emerging technologies such as engineering biology. The development of biocontainment systems will effectively minimize the risk associated with the emerging technologies, and to protect both the researchers and the wider community. It also provides a novel solution to combat intellectual espionage to safeguard our ever-growing bio-economy. This work is a great example of the responsible innovation of MIB research.”

Engineering biology is a relatively new, but expanding field of science that allows industry to use microorganisms, such as yeasts and bacteria, to produce value-added chemicals cheaply and efficiently. However, as microorganisms are often genetically engineered to increase efficacy, it becomes a problem if the organisms escape into the natural environment.

To ensure modified organisms do not find their way out of an laboratory setting, the NIH sets strict escape rate thresholds. Currently, most genetic safeguards rely on one of two methodologies to keep within the guidelines: either by engineering in an auxotrophy, whereby the organism relies on a specific metabolite to be present in its environment to survive, or a “suicide” gene, where the organism itself produces a toxin that kills it if certain conditions are not met.  

While these methods are generally genetically stable and effective enough to meet the NIH guidelines, they do have caveats to their efficacy. In the case of relying on a metabolite to sustain the organism, this metabolite may also be found in the wild and could not ensure the organism does not survive if it escapes. For “suicide” genes, as this is a direct threat to the organism, over generations the gene can selectively mutate and become inactive rendering it an ineffective control.

The new biocontainment method described by Hoffmann and Cai could be used in conjunction with the existing methods to bolster their effectiveness and deliver an even more robust escape frequency. Even if used as the sole biocontainment method, it provides an escape frequency of <2x10^-10 which far exceeds the NIH guideline of an escape rate of less than 10^-8.  

Today, the and The announced the nine recipients of the 2024 Blavatnik Awards for Young Scientists in the UK, including three Laureates and six finalists.

and are named among the three Laureates, who will each receive £100,000 in recognition of their work in Chemical Sciences and Physical Sciences & Engineering, respectively.

Now in its seventh year, the awards are the largest unrestricted prizes available to UK scientists aged 42 or younger. The awards recognise research that is transforming medicine, technology and our understanding of the world.

This year’s Laureates were selected by an independent jury of expert scientists from across the UK.

Professor Anthony Green, a Lecturer in Organic Chemistry from The University of Manchester, has been named the Chemical Sciences Laureate for his discoveries in designing and engineering new enzymes, with valuable catalytic functions previously unknown in nature that address societal needs. Recent examples include the development of biocatalysts to produce COVID-19 therapies to break down plastics, and to use visible light to drive chemical reactions. 

Rahul Nair, Professor of Materials Physics at The University of Manchester, was named Laureate in Physical Sciences & Engineering for developing novel membranes based on two-dimensional (2D) materials that will enable energy-efficient separation and filtration technologies. Using graphene and other 2D materials, his research aims to study the transport of water, organic molecules, and ions at the nanoscale, exploring its potential applications to address societal challenges, including water filtration and other separation technologies.

Internationally recognised by the scientific community, the Blavatnik Awards for Young Scientists are instrumental in expanding the engagement and recognition of young scientists and provide the support and encouragement needed to drive scientific innovation for the next generation.

, Founder and Chairman of Access Industries and Head of the Blavatnik Family Foundation, said: “Providing recognition and funding early in a scientist’s career can make the difference between discoveries that remain in the lab and those that make transformative scientific breakthroughs.

“We are proud that the Awards have promoted both UK science and the careers of many brilliant young scientists and we look forward to their additional discoveries in the years ahead.”

, President and CEO of The New York Academy of Sciences and Chair of the Awards’ Scientific Advisory Council, added: “From studying cancer to identifying water in far-off planets, to laying the groundwork for futuristic quantum communications systems, to making enzymes never seen before in a lab or in nature, this year’s Laureates and Finalists are pushing the boundaries of science and working to make the world a better place. Thank you to this year’s jury for sharing their time and expertise in selecting these daring and bold scientists as the winning Laureates and Finalists of the 2024 Blavatnik Awards for Young Scientists in the UK.”

The 2024 Blavatnik Awards in the UK Laureates and Finalists will be honoured at a black-tie gala dinner and award ceremony at Banqueting House in Whitehall, London, on 27 February 2024.

The Sustainable Commodity Chemicals through Enzyme Engineering and Design (SuCCEED) project will look to find new ways of manufacturing the chemicals needed for many every-day products through industrial biotechnology routes. By doing this, it will help the chemical manufacturing industry move away from fossil-based feedstocks and reduce their carbon footprint. 

Bio-based manufacturing routes are not currently widespread as they are difficult to scale up and don’t operate at the profit margins required for commodity chemicals. This poses a barrier to moving the chemicals industry away from petrochemicals and creating a greener industry. 

To help address this, the Prosperity Partnerships bring together industry and academia to find workable solutions to industry-based problems. The 91ֱ�� Institute of Biotechnology (MIB) and Shell have assembled an interdisciplinary team, led by , of biochemists, protein engineers, synthetic biologists, chemists, and chemical engineers to create a proof-of-principle, scalable, biorefinery. 

If successful, this 5-year project could help reshape the chemicals industry and support the UK delivering on its clean growth strategy.

Jeremy Shears, Chief Scientist for Biosciences at Shell said: “Shell aims to transition to a net-zero emissions energy business by 2050 and our work with the 91ֱ�� Institute of Biotechnology is important to unlock a more commercial route to sustainably produced chemicals. If we can demonstrate an effective route to bio-production, we hope this will be the catalyst for industrial change across the sector.”

Science, Research and Innovation Minister, Andrew Griffith, said:

“Our new bioscience prosperity partnerships are a valuable opportunity for government, business and academia to come together and help unleash world-class, pioneering discoveries across the UK while growing our local economies.

“More than £17m of Government funding is backing vital projects including work in Belfast to unearth life-saving drugs, in 91ֱ�� to improve skin health research and in Cambridge to tackle a major source of global pollution – enhancing the health and wellbeing of people across our country and beyond.”

Dr Lee Beniston FRSB, Associate Director for Industry Partnerships and Collaborative R&D at BBSRC, said:

“The inaugural round of the BBSRC prosperity partnerships programme has been a huge success. Led by BBSRC, with investment from our colleagues at MRC and EPSRC, we will invest more than £17 million in ten projects.

“This investment will support outstanding, long-term collaborative partnerships between businesses and academic researchers across the UK. Through the BBSRC prosperity partnerships programme, the businesses involved are investing over £21 million into research and development.

“The projects supported will deliver on UK ambitions for private sector investment in research and innovation as outlined in the Science and Technology Framework, helping to drive economic growth and societal impact through key bioscience and biotechnology sectors and industries.”

Industrial biotechnology uses nature’s own processes to produce value-added products, it is currently used to produce high-value chemicals such as pharmaceuticals. Enzymes and bacteria are the staple workhorses of biocatalysis – a process that speeds up chemical reactions – and can produce target chemicals by using anything from biomass to anthropogenic waste as a feedstock. Industrial biotechnology holds huge potential for creating a sustainable manufacturing environment and supporting the world’s transition to net zero.

The University was also successful in securing a second Prosperity Partnership with Boots, and co-leading a third with University College London.

MOOCs were set up in the mid-2000s to offer learning opportunities to distance learners. Since their inception they have brought education to thousands around the world, usually for free or at a low cost compared with traditional degrees. They have been credited with helping democratise higher education (HE) especially for those in developing nations by offering them a way to receive education from universities around the world, in a way and at a time that suits them.

The industrial biotechnology MOOC was designed and coordinated by Lesley-Ann Miller and Dr. Nicholas Weise from the 91ֱ�� Institute of Biotechnology, drawing together expertise from the University, and beyond, through a selection of contributors. The modules, which are all freely available worldwide to anyone with an internet connection, covers topics such as enzyme catalysis, synthetic biology, biochemical engineering, pharmaceutical synthesis, biomaterials, bioenergy and glycobiotechnology.  

The course exemplifies how industrial biotechnology can be used by society to meet global net zero goals and create more sustainable routes to manufacture of everyday products, as well as specialist chemicals used by industry. Since the Industrial Revolution, society has relied upon fossil fuels to provide the raw materials for many everyday products including pharmaceuticals, food and drink, materials, plastics, and personal care products.

With government targets drawing closer, industry must find new ways to manufacture these products without relying on finite resources. Industrial biotechnology offers a way for industry to adapt and change to meet these targets while still being able to produce high-quality and high-yielding products with a smaller impact on the environment.

Course instructors, Prof. Nicholas Turner, Dr. Nicholas Weise and Prof. Nigel Scruton, are delighted that the course has been used by hundreds of thousands as a way to access knowledge of sustainable bio-inspired technologies. The course is designed to help those looking to enter the field of biotechnology, upskill or even retrain to help solve technological challenges in their own areas. The course has received an average rating of 4.7/5.0 with learner stories such as:

Open dissemination of expertise from the University that can be used to solve global challenges is an important part of the research impact and social responsibility agenda for the university. The course has already received a recognition for its innovative practices in teaching and learning from the LearnSci Teaching Innovation Awards, a Teaching Excellence Award from the Institute of Teaching & Learning as well as being highly commended at the Making A Difference Awards for outstanding teaching innovation in social responsibility. 

This continued collaboration follows the successful completion of Phase-I of the development programme that centred on testing Luminspheres™-tracers under reservoir conditions in a laboratory setting.  Phase-II of the programme will validate multicoloured Luminspheres™ tracers under flow conditions.

Chromition’s system aims to offer an unprecedentedly detailed characterisation of complex geological environments and enable real-time monitoring of fluid flow between multiple wells facilitating proactive reservoir field management.

Mark McCairn, Chromition’s Chief Executive, said: “Shell’s continued commitment is a testament to the progress achieved to date in developing Chromition’s in-line tracer detection system, which for the first time will enable remote, real-time reservoir surveillance to improve the management of subsurface resources”.

Veronica Simmonds, Commercial Innovation Partnerships Manager/GameChanger, Shell, added: “We are very pleased with the technical progress made by Chromition during Phase-I and decided to grant an approval of the results and endorsement by the Shell GameChanger Tollgate Panel to continue to Phase-II of the programme with us”.

The Enzyme Discovery team won the Chemistry Biology Interface Horizon Prize: Rita and John Cornforth Award, while the Molecular Ratcheteers team won the Organic Chemistry Horizon Prize: Perkin Prize in Physical Organic Chemistry. 

The Enzyme Discovery team was recognised for its work investigating enzymes to combat antimicrobial resistance in the developing world. 

The team, based at the and the at The University of Manchester, with collaborators from GlaxoSmithKline, won the accolade for successfully discovering new enzymes for sustainable synthesis.

Their findings could lead to more affordable medicines, antibiotics that are more resistant to antimicrobial resistance, and even treat previously untreated diseases.  

Professor Jason Micklefield from the 91ֱ�� Institute of Biotechnology and the Department of Chemistry at The University of Manchester, said: “Our team is acutely aware of the importance of finding more sustainable and efficient routes to new and improved antimicrobials and other important therapeutic agents that are urgently required to combat antimicrobial resistance, treat diseases and tackle future pandemics.  

“Our research has allowed us to discover and engineer enzymes and pathways for sustainable synthesis, and we look forward to the future applications of our work in providing more parts of the world with increased access to essential medicines and more sustainable routes to commonly used products.”  

If adopted in industry, the Enzyme Discovery team’s work could lead to more affordable products, including medicines, which could be made more widely available to help combat antimicrobial resistance and other neglected diseases in the developing world. Their work also has the potential to help reduce other problems such as chemical waste. 

The Molecular Ratcheteers team was recognised for its work in nanotechnology, advancing the building blocks for everything from medicine delivery to information processing.

Based at the University of Manchester, with support from the University of Maine, the University of Luxembourg and East China Normal University, the Molecular Ratcheteers won the accolade for inventing engineering concepts that will help unlock the potential of the nanoworld.

The work leads to a variety of real-life applications like the creation of new nanomachines such as molecular motors, pumps and switches, that could make improvements in everything from the delivery of medicines to information processing. 

The group – which brought together minds with specialities in areas such as the physics of information and molecular biology – join a prestigious list of past winners in the RSC’s prize portfolio, 60 of whom have gone on to win Nobel Prizes for their work, including 2022 laureate Carolyn Bertozzi and 2019 laureate, John B Goodenough. 

Professor Dave Leigh from the Molecular Ratcheteers team at The University of Manchester, said: “It’s been fantastic to be part of such a talented team on the Molecular Ratcheteers project, and we’re proud to have developed concepts that could truly drive forward engineering in the nanoworld.” 

Miniaturisation has driven advances in technology through the ages. Early computers filled entire rooms and consumed vast amounts of energy yet had far less computing power than the tiny energy-frugal chips in today’s smartphones.

Making machinery smaller reduces power requirements, curtails the amounts of materials needed, cuts waste, facilitates recycling and produces faster operating systems. In doing so it advances technological progress while addressing the environmental and sustainability needs of society. 

Both research teams will also receive a trophy and a professionally produced video to celebrate the work. 

Dr Helen Pain, Chief Executive of the Royal Society of Chemistry, said: “The Horizon Prizes recognise brilliant teams and collaborations who are opening new directions and possibilities in their field, by combining their diversity of thought, experience and skills, to deliver scientific developments for the benefit of all of us.  

“The work of the Enzyme Discovery team is a fantastic example of why we celebrate great science; not only because of how they have expanded our understanding of the world around us, but also because of the incredible contribution they make to society as a whole. We are very proud to recognise their work.” 

The Royal Society of Chemistry’s prizes have recognised excellence in the chemical sciences for more than 150 years. In 2019, the organisation announced the biggest overhaul of this portfolio in its history, designed to better reflect modern scientific work and culture. 

The Horizon Prizes celebrate the most exciting, contemporary chemical science at the cutting edge of research and innovation.  

For more information about the Royal Society of Chemistry’s prizes portfolio, visit .

The research , demonstrates the high adsorption of benzene at low pressures and concentrations, as well as the efficient separation of benzene and cyclohexane. This was achieved by the design and successful preparation of two families of stable metal-organic framework (MOF) materials, named UiO-66 and MFM-300. These highly porous materials are made from metal nodes bridged by functionalised organic molecules that act as struts to form 3-dimensional lattices incorporating empty channels into which volatile compounds can enter.

VOCs such as benzene are common indoor air pollutants, showing increasing emissions from anthropogenic activities and causing many environmental problems. They are also linked with millions of premature deaths each year. Benzene is one of the most toxic VOCs, and is classified by the World Health Organization as a Group 1 carcinogen to humans.

“The really exciting thing about these materials is that they allow us not only to capture and remove benzene from the air, but also to separate benzene from cyclohexane, which is an important industrial product often prepared from benzene,” says Professor Martin Schröder, lead author of the paper which is published in . “Because of the small difference in their boiling points (just 0.6 ℃) the separation of benzene and cyclohexane is currently extremely difficult and expensive to achieve via distillation or other methods”.

Conventional adsorbents, such as activated carbons and zeolites, often suffer from structural disorder which can restrict their effectiveness in capturing benzene.  This new research also reports a comprehensive study of the adsorption of benzene and cyclohexane in these ultra-stable materials to afford a deep understanding of why and how they work.

“The crystalline nature of MOF materials enables the direct visualisation of the host-guest chemistry at the atomic scale using advanced diffraction and spectroscopic techniques,” says Professor Sihai Yang, another lead author of the paper. “Such fundamental understanding of the structure-property relationship is crucial to the design of new sorbent materials showing improved performance in benzene capture.”

The grant will begin the transformation of the University’s existing Pilot Plant for Chemical Engineering, creating a world-leading facility for sustainable chemical processing. This space will bring researchers together with industry professionals to provide the vital infrastructure needed to test advanced technologies that prototype industrial-scale processes.

91ֱ�� is the birthplace of Chemical Engineering, and the University continues to be a prime destination for industry‐relevant training. Today our academic researchers are at the forefront of some of the globe’s most transformational science and engineering discoveries.

Professor Lev Sarkisov, Head of the Department of Chemical Engineering has said about the project: “We are developing the new generation of sustainable chemical technologies by combining advanced concepts in multiscale modelling, materials, data science and process optimization.

"The new Industrial Hub will be the testing ground for these technologies at the pilot scale, accelerating their transition to the industrial practice. With the new facility, 91ֱ�� will lead research and innovation on clean energy working closely with industry and delivering a new curriculum for the next generation chemical engineers.”

The new Industrial Hub for Sustainable Chemical Engineering will be developed in the James Chadwick Building, which is part of the new £450m home for engineering and materials science - 91ֱ�� Engineering Campus Development (MECD) - opening in September 2022.

Professor Dame Nancy Rothwell, President and Vice-Chancellor of The University of Manchester, has said: “With support from the Wolfson Foundation, The University of Manchester will be able to significantly accelerate the UK’s ambitions for a thriving low carbon industrial sector. The new facilities will replicate industrial scale technologies and optimise industrial chemical processes, advancing scientific research to deliver solutions to the climate crisis.

We are excited to build on our position as the UK's primary university programme for the delivery of sustainable chemical engineering research and training the engineers of tomorrow.”

About the new home for engineering and materials science

91ֱ��’s new engineering and materials science development will provide world-class sustainable research facilities, alongside flexible and innovative teaching and learning spaces that will enable students to shape their own learning environment. It will house a community of 8,000 students, researchers, academics and professional services staff. This will be the largest concentration of interdisciplinary engineering expertise in any UK university.

Fuels such as this could be a way to bridge the gap between petrochemical derived fuels and cleaner energy sources. In industries such as aviation and shipping, where electrically powered vessels are currently impractical, advanced synthetic fuels offer a more sustainable alternative.

While not yet developed at an industrial scale, the team behind this advancement, which included colleagues from the Chemistry Department at The University of Manchester, were able to produce 15 litres of synthetic kerosene, enough to power a 4-meter drone for 20 minutes. Additionally, the process does not require any large-scale infrastructure and so can be made anywhere. This makes it an appealing prospect for companies and other stakeholders, including the RAF, as it could be rolled out across supply chains around the world.

With net zero and carbon emissions targets at the top of the global agenda, synthetic fuels will have a key part to play in countries achieving these goals. The RAF recently committed to finding more sustainable alternatives to fossil-derived aviation fuels, and with support from companies like C3 BIOTECH, they are one step closer to this. Eventually, similar fuel technologies will be available for commercial, as well as military applications which will further help to reduce the world’s carbon emissions.

Professor Sarah Haigh has been named winner of the Royal Society of Chemistry’s Analytical Division mid-career Award. Based at the University of Manchester, Professor Haigh won the prize for the development of transmission electron microscopy methods for advancing understanding of the dynamic behaviour of 2D materials and nanomaterials.

After receiving the prize, Professor Haigh said: “I’m very excited to have received this prize and thank the RSC for the honour. It is a testament to the hard work of my fantastic research group who very patiently put up with me. I am very grateful to them for their great ideas, persistence, enthusiasm, and collaboration. This prize is evidence that you can continue to succeed in science with a young family even with the huge additional challenges and stresses imposed by the pandemic over the last years.”

Most science and engineering processes occur in liquids or gases. Professor Haigh’s research group uses electron microscopes to study these processes, dynamically, with atomic spatial resolution and chemical sensitivity. Electron microscopes are similar to optical microscopes, but they use electrons instead of light. Electrons can be accelerated to very high speeds, when they have a wavelength 100,000 times smaller than visible light, which gives us the possibility to see atoms.

Applications of their research include studying the early stage synthesis of nanomaterials, the charging and discharging of batteries, the production of electricity from fuel cells or of green fuels from renewable energy, and the corrosion of pipelines or offshore wind turbines. Her research group is particularly interested in the applications for clean energy generation to support the net zero energy transition.

Professor Jason Micklefield has been named winner of the Royal Society of Chemistry’s Interdisciplinary Prize. Based at the University of Manchester, Professor Micklefield won the prize for innovative research spanning organic chemistry to molecular genetics, leading to the discovery, characterisation, and engineering of many novel enzymes.  

After receiving the prize, Professor Micklefield said: “I am very pleased to win this award. I am particularly grateful to my very talented research group for their hard work, dedication and excellent research over the years, which has made this possible.”

Nature uses enzymes to catalyse reactions building all of the molecules required for life. Enzymes also break down molecules to release energy that enables all living organisms to move forward. Professor Micklefield’s lab discovers novel enzymes from unusual bacteria in nature. They characterise these enzymes to determine their structures and mechanisms. With this knowledge, they are able to re-programme the enzymes to create variants that can catalyse new reactions. 

These engineered enzymes are used to produce novel antibiotics to combat antimicrobial resistance, antiviral agents that entered clinical trials for COVID-19, anticancer agents and other useful molecules. The enzymatic pathways they develop are cleaner and more sustainable than the traditional chemical synthesis routes that are currently used to prepare pharmaceuticals and other molecules.

Professor Christopher Hardacre has been named winner of the Royal Society of Chemistry’s Tilden Prize. Based at the University of Manchester, Professor Hardacre won the prize for outstanding contributions to the areas of liquid and gas phase heterogeneous catalysis.

After receiving the prize, Professor Hardacre said: “I was delighted and honoured but surprised.”

Professor Hardacre’s group focuses on the use of solids as catalysts for the production of commodity and fine chemicals and the removal of pollutants. Catalysts are materials that can lower the energy required for chemical reactions to proceed at the required rate. The group uses them in both the liquid phase and gas phase. The research aims to produce chemicals and fuels more efficiently and selectively. As well as having a direct application in the chemicals and energy sector, catalysis is key to achieving net zero.

Dr Helen Pain, Chief Executive of the Royal Society of Chemistry, said: “Great science changes the way we think about things – either through the techniques used, the findings themselves, the products that emerge or even in how we interact with the world and those around us. Importantly, it also allows us to reflect on the incredible people involved in this work and how they have achieved their results. 

“Although we are in the midst of negotiating a particularly turbulent and challenging era, it is important to celebrate successes and advances in understanding as genuine opportunities to improve our lives. The work of the three winners from The University of Manchester is a fantastic example of why we celebrate great science, and we’re very proud to recognise their contribution today.”

Reported in the journal, , a group of researchers from The University 91ֱ��, the European Commission Joint Research Centre Karlsruhe, and Los Alamos National Laboratory successfully prepared and characterised this long-sought transuranium chemical bonding scenario in an isolable compound.

The study of metal-element multiple bond interactions is an enormous area of research in chemistry with decades of intensive investigations that have sought to understand chemical bonding, reactivity, catalysis, and separations applications. Where actinide-element multiple bonding is concerned, there is much interest in exploiting understanding of chemical bonding (covalency) in extraction studies, because this could inform attempts to separate and clean up nuclear waste.

However, whilst metal-element multiple bond investigations are routinely reported and well established across the Periodic Table right up to uranium, the heaviest element to occur naturally in significant quantities, investigations involving transuranium elements, which are elements that come after uranium in the Periodic Table such as neptunium, have been restricted due to the need to conduct work on such radioactive elements in specialist facilities.

Inevitably with restricted experimental work for transuranium-element multiple bonding the transfer of knowledge from fundamental studies in this area to inform potential separations applications is low.

For the transuranium-element multiple bond chemistry that has been accomplished, examples that are known involve two or more element multiple bonds to a given transuranium ion in order to provide enough stabilisation to permit isolation of those compounds. However, the presence of two or more multiple bonded elements has meant that such linkages could not be studied in isolation, complicating their analysis. To date it had not been possible to access transuranium complexes with just one multiple bond to an element that was stable enough to be isolated, so it has been impossible to reliably experimentally confirm or disprove theoretical predictions, which is difficult to do generally for elements that are in relativistic situations.

Using specialist handling facilities, the researchers succeeded in preparing a complex containing a neptunium ion with a multiple bond to a single oxygen atom. The key to success was careful design of the supporting, cage-like organic ligand framework with four stabilising nitrogen donors and large silicon-based flanking groups to protect the neptunium-oxygen bond and enable its study in isolation.

By extending from prior work on uranium now to neptunium, the researchers were able to make hitherto impossible comparisons, with the surprise finding that the neptunium-oxygen complex has more covalent chemical bonding that an isostructural uranium-oxygen complex. This is the opposite of predictions, underscoring the difficulty of making predictions in this area of the Periodic Table and the importance of experimentally testing them.

Professor Steve Liddle, co-Director of the Centre for Radiochemistry at The University of Manchester, coordinated the research. He said: “It is thanks to the talent of the researchers involved in this study and through collaboration at specialist facilities internationally that this work has been possible.

Molecular uranium and thorium chemistry has taken enormous strides forwards in recent years through the study of metal-element multiple bonding, but transuranium science has lagged far behind due to the challenges of working experimentally with these elements. The researcher’s work demonstrates that transuranium analogues are now accessible for wider study, opening up opportunities to grow this new field of actinide science.

The paper, ‘A terminal neptunium(V)–mono(oxo) complex’, is published in .

Researchers from (MIB), led by Professor Nicholas Turner, Dr Sarah Lovelock and Professor Anthony Green, have developed an efficient biocatalytic manufacturing route to Molnupiravir. Experimental work was led by Dr Ashleigh Burke who developed a new enzyme, cytidine aminotransferase, to allow the production of a key Molnupiravir intermediate.

The unique approach of the 91ֱ�� team is currently being further developed with industrial partners at multi-Kg scale to enable adoption by generic pharmaceutical manufacturers at large scale.

Professor Anthony Green said: “We are hopeful that our work will contribute to the challenge of developing a low-cost manufacturing route to Molnupiravir to allow the widest possible access to this promising COVID-19 therapy.”

The research undertaken by The University of Manchester team has been to allow pharmaceutical manufacturers around the world to take advantage of this development.

Sterling Pharma Solutions, a pharmaceutical contract development and manufacturing organisation (CDMO), has been engaged to support scale-up development and manufacturing activities utilising the novel enzyme developed by the 91ֱ�� team. Sterling’s CEO, Kevin Cook, said: “We are incredibly proud to be working in partnership will all those involved to help improve global access to what looks to be a very promising, life-saving treatment.”

In order to maximise the impact of the new enzyme technology, Prozomix Ltd, a biocatalyst discovery and contract manufacturing organisation (CMO), will employ foundation funds to produce high-quality cytidine aminotransferase and distribute it globally free-of-charge. Any company can obtain a sample by emailing Molnupiravir@prozomix.com.

Prozomix's Managing Director, Professor Simon Charnock, said: "Establishing a new and widely employable biocatalytic route for an API has arguably never been as urgent, we feel most privileged to play our part in this collaboration."

The SynHiSel programme has received a total of £9m in funding, from the , part of UK Research and Innovation, and from industrial and University partners.

The project, the biggest of its kind to date, will investigate how to develop more efficient ways of separating chemicals – processes that underpin crucial parts of everyday life including clean water treatment, CO₂ removal and food and pharmaceutical production.

It is estimated that these separations currently consume 10-15 percent of total energy usage, and that they could be made 10 times more efficient by creating new highly selective membranes. This could cut annual worldwide carbon dioxide emissions by 100 million tonnes and save £3.5 billion in energy costs.

Professor Peter Budd, The University of Manchester said: “Both scientific ingenuity and engineering skill are needed in the development of new membranes and processes for sustainable and efficient separations. We are delighted to be working with some wonderful collaborators to explore new opportunities for membrane technology.”

The programme’s principal investigator Professor Davide Mattia, of the says the project aims to help the UK lead in developing new high value, high efficiency chemical processing techniques.

Prof Mattia says: “Some of the biggest challenges we face – how to develop drugs and vaccines, ensure food security and quality, and how to make sure the water we drink is clean – all require some form of chemical separation. We want to improve our understanding of highly selective membrane technology to create value in manufacturing and make processes more sustainable.”

The University of Manchester has a proud record of developing innovative materials that offer the prospect of membranes with unprecedented selectivity and productivity for molecular separations on a large scale. Highly permeable polymers referred to as ‘Polymers of Intrinsic Microporosity’ (PIMS) invented by chemists in 91ֱ�� nearly 20 years ago, are at the forefront of research into efficient gas separations. Graphene, first isolated by physicists at 91ֱ�� around the same time, has led to graphene-based membranes with enormous potential for producing clean water from dirty water.

Through the SynHiSel programme grant, researchers in chemistry and chemical engineering at The University of Manchester will work together with membrane scientists across the UK to help tackle global challenges such as cleaning our air, cleaning our water, and enabling industry to operate more sustainably. A focus on real-world applications is facilitated by the support of industrial partners ranging from multinational companies to small enterprises such as the 91ֱ�� spin-out, .

The programme will bring together chemical and process engineers, chemists, materials scientists and experts in scaling-up of industrial manufacture. Prof Mattia says that this breadth of expertise will allow the team to be more inventive in its approach.

Ian Metcalfe, Professor of Chemical Engineering at Newcastle University and deputy director of the programme, added: ‘Our membrane work was originally funded by an earlier EPSRC Programme Grant, SynFabFun, which was a great success. It is wonderful to see the team develop, to bring in new investigators and to move on to new challenges as SynHiSel.”

As well as new scientific innovation, the SynHiSel programme aims to develop a new generation of talent in the field, by acting as the virtual UK national membrane centre. The academic and industrial partners will create an initial cohort of 11 new PhD studentships, and PhDs and post-doctoral research associates will gain valuable experience as part of the multidisciplinary research groups and be given dedicated training and professional development opportunities.

Industrial partners including Evonik Industries AG, Dupont Teijing Films (UK), Pall Europe, BP, ExxonMobil, and Cytiva Europe will work with the team to ensure the industrial potential of the new processes and tools they develop. UK-based SMEs including Exactmer, Nanotherics, RFC Power, Watercycle Technologies, Laser Micromachining and the University of Bath spinout Naturbeads will also collaborate with the programme research team.

The SynHiSel programme team comprises: Prof Davide Mattia and Prof John Chew, University of Bath; Dr Patricia Gorgojo and Prof Peter Budd, University of Manchester; Prof Ian Metcalfe and Dr Greg Mutch, Newcastle University; Prof Neil McKeown and Prof Maria-Chiara Ferrari, University of Edinburgh; Prof Andrew Livingston, Queen Mary University of London; Prof Kang Li and Dr Qilei Song, Imperial College London.

This highly coveted prize is awarded annually to independently funded students for "a record of outstanding accomplishments during their PhD in any discipline" and is the highest award given to graduate students studying outside China.

During his PhD, which was funded by the University of Manchester President’s Doctoral Scholarship Scheme, Jinzghen investigated the chemistry of actinide-nitrides, probing their synthesis, electronic structure, and reactivity, and unusual small molecule activation at transient low-valent thorium. After his PhD, Jingzhen remained in the Liddle Group where he is currently a postdoctoral researcher.

Jingzhen said: “I am absolutely humbled and delighted to be a recipient of this award. The list of previous winners is full of highly talented individuals, so I am deeply honoured to have been selected.”

of the has been named a recipient of the highly prestigious .

The coveted prize is awarded on the authority of Her Majesty The Queen; and Professor Leigh receives the medal for his work in scientific research, along with Professor Andrew Morris of the University of Edinburgh.

Professor Leigh is recognised for his pioneering work in methods to control molecular-level dynamics. His body of work on the synthesis of entwined and entangled molecular systems – such as threads, knots, and links – has been ground-breaking, and has enabled advancement of synthetic molecular machines (nanobots).

He said: "I'm delighted and humbled to be awarded a Royal Medal from the RSE. The list of past recipients of RSE Royal Medals reads like a roll call of the highest distinction in Scottish life, encompassing the sciences, arts, business and public service, and to have my name added to them now is an immense honour."

The RSE recognises excellence through awarding several medals – the most prestigious of which is the RSE Royal Medal.

The newly published findings are the result of collaborative work between Global Bioenergies and the team of Dr. David Leys at The University of Manchester, and have been published today in . This paper describes the evolution and mechanism of isobutene forming enzymes far superior to previously used catalysts. Isobutene is a high value gaseous hydrocarbon, and one of the major building blocks of the petrochemicals industry: 15 million tonnes are produced every year to yield cosmetic ingredients, rubber and fuels.

This is the first time a member of a widespread enzyme family that depends on an unusual vitamin B2 derivative has been repurposed to yield isobutene. This has been made possible through the extensive work performed on both sides of the Channel, with laboratory guided evolution carried out at Global Bioenergies, and detailed structure analysis of the the evolved enzymes at The University of Manchester.

David Leys, group leader at the 91ֱ�� Institute of Biotechnology of The University of Manchester, says: “Our collaboration with Global Bioenergies on the subject of isobutene production combines in a unique manner quantitative molecular bioscience and industrial, high-throughput approaches. It is very satisfying to see how fundamental understanding of these enzymes obtained with European Research Council funding supports industrial application. The evolved enzymes represent several orders of magnitude improvement in the efficiency of isobutene bioproduction, directly contributing to an economically viable and renewable process, and thus a more sustainable future.”

Marc Delcourt, co-founder and CEO of Global Bioenergies, adds: “Nature Communications stands among the high-class peer-reviewed scientific journals. We are very pleased to see the work we conducted jointly with the team of Dr David Leys reaches such a striking scientific recognition. The evolved enzymes, on which GBE holds exclusive intellectual property rights for the isobutene production, will have a significant role in the environmental transition our world is now engaged in.”

As an alternative to fossil fuel derived isobutene, Global Bioenergies assembled a modified pathway for the production of isobutene from glucose. The crucial final step yielding the desired product makes use of a decarboxylase enzyme. This particular enzyme has been evolved from naturally occuring microbial decarboxylases that depend on an elaborately modified Vitamin B2 (called prenylated flavin or prFMN) for activity.

The 91ֱ�� group has been at the forefront of studying these prFMN-dependent catalysts, and determined structure and biochemical properties of isobutene yielding enzymes evolved by Global Bioenergies. The company screened an enzyme library for inherent isobutene production activity, and used directed evolution to yields variants with up to an 80-fold increase in activity. Structure determination of the evolved catalysts reveal that changes in the enzyme pocket are responsible for improved production, while solution and computational studies suggest that isobutene release is currently the limiting factor.

Global Bioenergies has developed a unique conversion process for renewable resources into isobutene, one of the main petrochemical building blocks that can be converted into ingredients for cosmetics, petrol, kerosene, LPG and plastics.

Reported in the journal , a group of scientists from 91ֱ�� and Stuttgart universities have successfully prepared and characterised long-sought actinide-actinide bonding in an isolable compound.

The majority of the Periodic Table is metals, so the field of metal-metal bonding is a vast area of research after nearly 180 years of investigations, with applications spanning understanding electronic structure, catalysis, chemistry at metal surfaces, magnetism, and bio-inorganic chemistry. Bulk materials can be difficult to study, so there is great interest in studying molecular compounds possessing metal-metal bonding, since such species can be more straightforwardly studied in detail and they constitute models that represent molecular fragments of bulk materials.

Though metal-metal bonding is extremely well developed for transition metals and main group elements, which has served as the foundation of the above applications, it has remained virtually unknown for the actinide elements, with examples restricted to spectroscopically observed transients or fundamental diatomics in microscopic-scale trapping experiments. Furthermore, making predictions about elements in the relativistic regime at the foot of the Periodic Table is highly challenging. Thus, experimental realisation of actinide-actinide bonding in routinely isolable molecules has been one of the top targets of synthetic actinide chemistry for decades.

The researchers succeeded in preparing a reduced, that is electron-rich, trithorium cluster. Had conventional reducing reagents been used the result would have been missed, because those heterogeneous reagents produce the trithorium cluster slowly, so only trace quantities are present at any one time due to decomposition during extended reaction times. However, the key to success was using a soluble homogeneous reducing reagent that gives almost instantaneous reactions affording the trithorium cluster in high isolated yield before it can decompose.

Professor Steve Liddle, co-Director of the (CRR) at The University of Manchester, led the research. He said: “By using just the right reducing agent combined with the right synthetic precursor, we were able to isolate a complex that would otherwise have certainly eluded us, which raises the interesting question of whether other actinide-actinide bonding has evaded the field before but could now be accessible.”

Surprisingly, using a range of characterisation techniques, the researchers found that at the heart of the molecule there resides two paired electrons in a cloud of electron density that is shared equally between the three thorium atoms. This very rare situation is called sigma-aromatic bonding, and its report here extends this type of bonding to a record sixth principal atomic quantum shell and to the seventh row of the periodic table.

The trithorium cluster is notable on two further counts. Firstly, it contains actinide-actinide bonding that can be made at scale and isolated, which will permit wider development and understanding of it and its chemistry, opening up this new field. Secondly, the sigma-aromatic bonding runs counter to the vast majority of prior theoretical predictions and experimentally realised metal-metal bonding, highlighting the difficulties of making predictions about relativistic systems.

Fellow CRR co-Director Professor Nikolas Kaltsoyannis led the computational analysis. He said: “The chemical bonding in this beautiful molecule is exquisitely unexpected, underscoring just how unpredictable the actinide elements can be.”

The ability to now make and isolate actinide-actinide bonded compounds, whose reactivity and properties can be now straightforwardly examined, opens up opportunities to grow this new area of metal-metal bond chemistry, for example providing models for bulk actinide materials and potentially new quantum behaviours.

The key topics that will be discussed include:

• Emerging trends in research and development
• Data reporting, survey and statistics
• Analysis of sectors including life sciences, manufacturing, agriculture, and energy
• Emerging technologies, such as automation, AI and VR

Professor Scrutton will be joined by policymakers such as Nadhim Zahawi MP, Minister for BEIS and COVID-19 Vaccine Deployment, and Chi Onwurah MP, Shadow Minister for Science, Research and Digital, as well as business leaders such as Andy Topping, Chief Scientific Officer at Fujifilm Diosynth Biotechnologies, and sector specialists such as Professor Lionel Clarke, Chair of the UK Synthetic Biology Leadership Council.

The live panel and Q&A will discuss how UK industry - responsible for a quarter of the UK's greenhouse gas emissions - can use biotechnology to reduce its carbon footprint and contribute to the UK's net zero goals. Specifically, they will focus on how biotechnology can create more sustainable chemicals for agriculture, more efficient and greener fuels for transport, and close the gap in our economy to create a circular economy.

The event will start at 2.30pm on Thursday, 15 July. To book tickets, please .

For more information about how The University of Manchester’s biotechnology research is supporting the UK's net zero goals, please visit the net zero campaign page.

Biotechnology is one of the University's research beacons - examples of pioneering discoveries, interdisciplinary collaboration and cross-sector partnerships that are tackling some of the biggest challenges facing the planet.

Each of the staff-based awards (ten in total) included an individual from the Department shortlisted as the top three nominations across the University - out of more than 315 nominations in total. From this, the Department received a total of four awards.

Dr Alan Brisdon received the award for Innovative Teaching; Jessica Hingley and Jennifer Managh received the award for Excellent Support Staff; Dr Nicholas Weise received the award for Commitment to Student Partnership; and Wanpeng Lu from the Yang Group received the Award for Outstanding Graduate Teaching Assistant.

Professor David Mills was shortlisted to the top three nominations under both Above and Beyond, as well as Excellent Academic Advising; Dr Sihai Yang was shortlisted to the top three nominations for Exceptional Feedback and Outstanding Postgraduate Supervision; Professor David Collison was in the top three for Inclusive Teaching Practice; and Dr Frank Mair was in the top three for Diversity in the Curriculum.

The Scheme was the runner up in the Innovator Category, and Shamael, Klara, Dukula, Mariam, Nelly, Oscar and Dr Nick Weise also received Outstanding Contribution Awards for their roles in Peer Support.

The Royal Society of Chemistry’s prizes have recognised excellence in the chemical sciences for more than 150 years. In 2019, the organisation announced the biggest overhaul of this portfolio in its history, designed to better reflect modern science.

Of those to have won a Royal Society of Chemistry Prize, over 50 have gone on to win Nobel Prizes for their pioneering work.

The 91ֱ�� recipients have been awarded for research themes ranging from diagnosing Parkinson’s disease and molecular magnetism, to developing new biocatalysts for pharmaceuticals.

The University of Manchester award winners:

• The Nose-to-Diagnose Team of Universities of Manchester and Edinburgh, with collaborators in the Netherlands and in Industry, have been named the winner of the Royal Society of Chemistry’s new Analytical Division Horizon Prize: Robert Boyle Prize for Analytical Science.
• The Molecular Magnetism Group from The University of Manchester has been named the winner of the Royal Society of Chemistry’s new Dalton Division Horizon Prize.
• The CrystalGrower team – an international team led by scientists from the University of Manchester, has been named the winner of the Royal Society of Chemistry’s new Materials Chemistry Division Horizon Prize.
• The Biocatalyst Discovery team – also known as the Redam Detectives – has been named the winner of Chemistry Biology Interface Division Horizon Prize: Rita and John Cornforth Award.
• The teams become four of the first winners of the Royal Society of Chemistry’s new Horizon Prizes, introduced after the organisation carried out a wholesale review of its recognition portfolio to better reflect modern science and its impacts in making the world a better place.
• Dr Jiangnan Li is the winner of the Royal Society of Chemistry’s Dalton Emerging Researcher Award.
• Dr Nicholas Chilton is the winner of the Royal Society of Chemistry’s Harrison-Meldola Memorial Prize.
• Dr Helen Ryder is the winner of the Royal Society of Chemistry’s Award for Exceptional Service.

The Horizon Prizes celebrate the most exciting, contemporary chemical science at the cutting edge of research and innovation. These prizes are for teams or collaborations who are opening up new directions and possibilities in their field, through ground-breaking scientific developments. The teams receive a trophy and a professionally produced multimedia pack showcasing the prize-winning work and its importance.

The Horizon Prizes celebrate the most exciting, contemporary chemical science at the cutting edge of research and innovation. These prizes are for teams or collaborations who are opening up new directions and possibilities in their field, through ground-breaking scientific developments. The teams receive a trophy and a professionally produced multimedia pack showcasing the prize-winning work and its importance.

The Research and Innovation Prizes – of which the Dalton Emerging Researcher Award and the Harrison-Meldola Memorial Prize are two – celebrate brilliant individuals across industry and academia. They include prizes for those at different career stages in general chemistry and for those working in specific fields, as well as interdisciplinary prizes and prizes for those in specific roles.

The Volunteer Recognition Prizes – of which the Award for Exceptional Service is one – celebrate those who give their time freely in numerous ways, from serving on boards and committees to working on public engagement initiatives. The prizes celebrate teams and individuals at all stages of their career.

After receiving the prize, Professor Perdita Barran, Chair of Mass Spectrometry and Director of the Michael Barber Centre for Collaborative Mass Spectrometry, The University of Manchester, said: “We say we are led by the nose and we are, although all of this has been a route to exploring sebum which has been tremendously exciting because we believe sebum traps compounds. From the smell of new-born babies to the scent of second-hand clothes, we all have a knowledge that sebum has a smell or can trap smells, but Joy was the person who made us realise that this could be useful. When you think of it like that – you wonder why no one thought of it before.”

The team receiving the prize for contributions to molecular magnetism, was led by Professor Richard Winpenny, Synthesis and Measurement, EPSRC Established Career Fellow, The University of Manchester.

After receiving the prize, he said: “We’re delighted that the team is being recognised and not just individual group leaders. It is a great initiative of the Royal Society of Chemistry to bring in a prize that recognises our culture that brings together team members with different skills to address interdisciplinary challenges.”

Dr Ryder, Chair of the Royal Society of Chemistry's Formulation Science and Technology Interest Group (FSTG), won the prize for outstanding service to the Royal Society of Chemistry.

On receiving the prize, Dr Ryder said: “What an honour! I am extremely proud to accept this Award for Exceptional Service from the RSC. To be recognised for the voluntary work I do as Chair of the Formulation Science and Technology Interest Group and as Interest Group Representative for the Member Networks Committee is truly amazing. There are so many fantastic volunteers working to advance the chemical sciences so to be nominated and awarded this prestigious award is beyond anything I thought possible. Truly, truly grateful.”

The team's winning idea was a fictional business (EKKO) that could tackle the problem of fatbergs. Fatbergs have had a high media profile over the last few years, with many causing issues in large cities all over the world. Fatbergs are caused by the build-up of fat and grease, combined with other "non-flushable" products combining into a solid mass that blocks up sewers.

The current solution for fatbergs is to send people into the sewer to break them up and then dispose of the waste in landfills. With so much other waste going to landfill, this solution is not sustainable long-term. This is where the competition team had the idea of using engineered yeast to break down the fatbergs into useful products such as single cell protein and oil as sustainable alternatives to conventional fish feed.

"While our company is fictional, the science behind it is real" says Oksana Bilyk, one of the researchers on the winning team, "if we could turn a big problem like fatbergs into something useful, it could have huge socioeconomic impact".

Current fishmeal is produced by using wild-caught fish which has significant environmental problems for marine ecosystems. If a yeast could be developed to break down fatbergs, then it would no longer be necessary to deplete wild fish stocks to raise captive commercial fish.

The North West Biotech Initiative (NBI) business idea competition is an annual competition run by the NBI that is designed to give students entrepreneurial experience, something that team EKKO were keen to develop.

"During the workshops we learned a lot about what it takes to develop and run a business. The competition has helped us to rethink how we approach science and look at how we can build a commercial product from the work we are doing." says team captain Erik Hanko.

The NBI is a platform that supports students to meet and work with local and international businesses and industry experts. Founded in 2014 by two PhD students, the NBI has gone on to connect not only post-graduates but those earlier in their academic careers with businesses and industry professionals.

Kris Valdehuesa says of the competition; "We're really grateful for this experience, the competition has been a perfect opportunity to learn what it takes to be successful in business and we're really glad we took part".

New research published today, in , demonstrates a new way of merging natural and synthetic catalysts to deliver more efficient and sustainable routes to pharmaceuticals and other valuable chemical products.

Currently chemical synthesis is used to construct many of the molecules that we rely on, from medicines that combat disease and agrochemicals to boost crop yields, through to plastics and other materials that are used in all aspects of daily life.

It is widely recognised that these traditional chemical processes are increasingly unsustainable, relying on non-renewable ingredients, highly toxic or otherwise deleterious reagents and solvents, and can create harmful emissions and waste streams.

Chemicals production also relies on multi-step synthetic routes that are expensive, meaning that many valuable products, including some essential medicines are only available to a privileged few within affluent nations.

To address these major problems, a team of chemists from The University of Manchester have devised a way of combing natural and synthetic catalysts to speed up the chemical manufacturing process.

who led the study said: “We are optimistic that the new integrated catalytic processes we have developed could lead to cleaner, safer and more cost-effective ways to make chemical products, such as new pharmaceuticals, which is important for a more sustainable future.

“We used bacterial cells with the enzyme produced inside. In this way the cell membrane prevents the enzyme coming into contact with the metal catalyst but allows the small molecule building blocks to flow through. We also deployed enzymes in a membrane made of cross-linked fibres, from wood pulp, rather like a tea bag but with smaller holes, which allowed us to remove and recycle the enzymes.”

“The main advantage is that everything is done in water which is clean and safe. Most of the current processes use organic solvents which are toxic, flammable and dangerous to the user and the environment. The use of multiple catalysts also means that we do not need to use additional dangerous and undesirable chemical reagents (acids, bases & oxidising agents etc.) which are typically required in traditional processes.”

The scientists used enzymes (natural protein catalysts) that had been modified to improve their properties together with non-natural metal catalysts. Normally it is not feasible to use these different types of catalysts together as they deactivate one another and consequently they would be deployed in separate laborious and costly multi-steps processes.

To overcome these compatibility issues, the team developed ways to compartmentalise the different catalysts, so that they could be used in a single integrated process. Rather than using typical toxic chemical reagents and solvents, the new integrated processes can be performed in water, to deliver pharmaceuticals and other target products by a more direct, environmentally friendly and cheaper route.

Various enzymes were used, but the key enzyme was a halogenase enzyme which installs halogen atoms (chlorine or bromine) into the precursors (building blocks). The halogen atoms are reactive and can be used create new bonds between the build blocks enabling the assembly of larger molecules. Mutations were then introduced into the haloganese enzyme changing its shape so that it could accept a wider range of different building blocks. 

The new research details a way to make molecules more cleanly, safely and efficiently in fewer steps. If adopted in industry, it would reduce problems of chemical waste and potentially lead to more affordable products, including medicines which could be made more widely available to help treat antimicrobial resistance (AMR) and neglected diseases in the developing world along with antiviral agents to deal with the threat of current and new viral pandemics. All of which are currently expensive produce as they are manufactured by laborious multi-step routes.

Professor Nigel Scrutton, who heads up the EPSRC-funded UK Future Biomanufacturing Research Hub and the BBSRC Synthetic Biology Research Centre "SYNBIOCHEM", has been appointed to the UKRI-BBSRC council for a term of three years.

The Biotechnology and Biological Sciences Research Council (BBSRC) is part of UK Research and Innovation (UKRI) which invests in biosciences research and training to support the economy, job creation, and to improve quality of life not only in the UK but on a global level.

The BBSRC council is responsible for advising and making decisions across its key discipline areas including budgeting and delivering plans for research and innovation; ensuring there are future generations of skilled specialists and scientists to support the UK research and innovation sector; engaging with communities and disseminating information; and encouraging collaborative work across the nine UKRI councils.

Speaking about the appointment, Professor Scrutton said:

Professor Scrutton brings a wide range of biochemistry and senior leadership skills to the BBSRC. Most recently he was the Director of the 91ֱ�� Institute of Biotechnology, for which he and the Institute were recognised for their work with a Queen's Anniversary Prize. He was elected a Fellow of the Royal Society (FRS) in 2020 and has held a professorship at the University since 2005, previously holding the position of Associate Dean for Research in the Faculty of Biology Medicine and Health (formerly the Faculty of Life Sciences).

Through his directorship of the University Centres of Excellence - SYNBIOCHEM and FutureBRH - and spin-out company C3 BioTechnologies Ltd, his work spans areas such as enzyme chemistry, biophysical methods, and structural and synthetic biology, that contribute to understanding the chemistry of life. Through the world-leading infrastructure for biophysical chemistry and synthetic biology at the University, Professor Scrutton's work takes an interdisciplinary approach to solving some of today's grand challenges.

Industrial biotechnology is one of the five research beacons at The University of Manchester, which are examples of interdisciplinary and pioneering research that are finding solutions to global problems. #ResearchBeacons.

The online events will take place throughout the week commencing Monday, 14 December as part of wider celebrations across The University of Manchester. They will provide an opportunity for both staff and students to mark winter graduation after physical ceremonies were postponed due to the ongoing COVID-19 pandemic.

FSE graduation celebrations will be spread over the week, with events held for mathematics; mechanical, aerospace and civil engineering (MACE) - technical; MACE - management of projects; physics and astronomy; electrical and electronic engineering; international fashion retailing; materials science and engineering; chemical engineering and analytical science; earth and environmental sciences; computer science; and chemistry.

The move online means students will be able to celebrate regardless of where they are currently situated. It shows that while they may not be in the city at the moment, 91ֱ�� is behind its graduates as they take their next steps out into the world.

Each subject area will celebrate in its own unique way - either via YouTube or Zoom. Dates and times - and links to those on YouTube - are provided below:

School of Engineering

• - Wednesday, 16 December, 11.30am
• - Wednesday, 16 December, 9am
• - Thursday, 17 December, 11.30am
• - Friday, 18 December, 12pm
• - Friday, 18 December, 10am

School of Natural Sciences

• Chemistry - Thursday, 17 December, 11am (link available soon)
• Earth and environmental sciences - Monday, 14 December, 10am (link available soon)
• Materials: International fashion retailing - Wednesday, 16 December, 2pm (link available soon)
• Materials science and engineering - Tuesday, 15 December, 2pm (link available soon)
• Mathematics - Wednesday, 16 December, 10am (link available after the event) 
• Physics and astronomy - Tuesday, 15 December, 11am (link available after the event)

A huge congratulations to all of our FSE graduates, and the best of luck for the future!

Announced today (Wednesday, 9 December) by the and the , of the is one of three Laureates from UK universities who will each receive $100,000 (£76,000) for their work across life sciences, physical sciences and engineering, and chemistry.

Now in its fourth year, the award is the largest cash prize available to scientists aged 42 or younger. The recipients are recognised for their research, which is already transforming technology and our understanding of the world.

, also of the Department of Chemistry, and of the have been named among this year's Finalists, and will both receive $30,000 (£23,000).

Professor Leonori has been honoured for the development of new methods for the formation of chemical bonds between atoms of carbon and nitrogen. His techniques have revolutionised the synthesis of complex molecules by employing photocatalysis - a method to expedite chemical reactions using visible light.

He says: "My research focuses on inventing new photocatalytic pathways to prepare nitrogenated molecules like drugs and agrochemicals. I am deeply honored to be named the Blavatnik Laureate in Chemistry for the United Kingdom and I owe this success to my outstanding students and postdoctoral researchers. It is their hard work and continuous ability to surprise me with new ways to look at chemistry that has led to all of our major discoveries."

Dr Mills is recognised for making a critical discovery that has revitalised the field of single-molecule magnets, paving the way for their practical use. These single-molecule magnets have potential applications in high-density data storage and quantum computing.

"I am both humbled and delighted to be selected as a Blavatnik Awards honoree in recognition of the combined work of my group and our collaborators over the last eight years. I'd like to take this opportunity to thank family, friends, colleagues and mentors for their continued help and support. Our group at 91ֱ�� continues to target making and measuring challenging molecules that have no right to exist, which inspires me on a daily basis," Dr Mills explains.

Professor Mishchenko has been recognised for revealing unusual quantum phenomena in vertical, multilayer stacks of two-dimensional materials, in particular those that hold great potential in the development of novel electronic transistors for light-emitting diodes (LEDs), high-speed electronics, and information storage.

He says: "Two-dimensional crystals can be assembled in a very precise way into van der Waals heterostructures. This recent van der Waals technology allows creating designer materials with endless possibilities for discovery of novel physics with a promise of numerous potential applications. I am proud that I contribute to this exciting research direction and want to thank all the collaborators and colleagues for their help and support."

The Laureates and Finalists will be honoured, as pandemic restrictions allow, at a black-tie gala dinner and ceremony at Banqueting House in London, tentatively scheduled for 8 June 2021. The following day the honourees will present their research with a series of short, interactive lectures at a free public symposium entitled 'Innovating for a Better Future: Nine Young Scientists Transforming our World'.

Researchers from The University of Manchester have discovered that simple manipulations of carbon nitride, a metal-free, non-toxic solid, made of Earth abundant elements of carbon and nitrogen, are able to efficiently exploit solar light for the synthesis of organic molecules containing fluorine, which are the building blocks of many agro-chemical and pharmaceutical applications.

The concept the scientists used is known as ‘photocatalysis’ whereby artificial light or sunlight is able to trigger chemical reactions at ambient conditions, which would otherwise require more energy intensive processes.

The process can be compared to that of natural photosynthesis used by plants to harness the sun’s energy. However, artificial exploitation of light energy is very challenging as materials used for this purpose are generally very expensive, difficult to make and very often not efficient in triggering chemical reactions. This represents a major issue in terms of process viability on a large scale.

Industrial implementation of photocatalytic process would be hugely beneficial for the environment and society as it would be able to provide cleaner and more sustainable chemical products reducing and potentially removing the use of fossil fuels as primary source of energy in such industrial productions.

The new findings which are published today in the journal , are the result of an international collaboration between Dr Carmine D’Agostino at The University of Manchester (UK), with The University of Trieste (Italy), together with the CNR Institute of Materials for Electronics and Magnetism (Italy) and the CIC biomaGUNE (Spain).

The team at The University of Manchester led by Dr Carmine D’Agostino, together with Luke Forster (PhD student) and Dr Graziano Di Carmine (Research Associate) played a pivotal role in unravelling, through the use of Nuclear Magnetic Resonance (NMR) techniques, the fundamental changes in carbon nitride properties responsible for the increased efficiency of the nano-engineered materials.

Dr Carmine D’Agostino said: “The chemical industry is a fundamental pillar for economic and technological development. Yet, it is often associated with environmental pollution and climate change. In recent years, efforts are being made to shift the current approach to industrial chemistry towards a greener, more sustainable and zero-waste approach.”

“This new exploitation of solar light for synthesis of useful chemicals is a very promising technology, yet very challenging. In particular, the search of non-toxic, widely available and economically viable materials, able to harness solar energy for efficient chemical conversion holds the Holy Grail for such photochemical conversions.”

This discovery paves new ways for the sustainable synthesis of a wide range of molecules of interest for the pharmaceutical and food industries and puts the basis for a new approach towards modern industrial chemistry.

A group of chemists from 91ֱ�� have successfully tied a series of microscopic knots using individual molecules for the first time, ushering in the advent of a form of nano-scale weaving which could create a new generation of advanced materials.

The group based at The University of Manchester have developed a way to tie an artificial 15 nanometre (15 millionths of a millimetre) molecular strand into any one of three different knots just as if using a piece of string.

A piece of string can be tied into different knots, some with distinctive properties that can be exploited for different functions from shoelaces to nooses, hitches, bends and stopper knots. Some of the most advanced equipment ever developed, including the used on Mars, use knots to perform key tasks. Although some DNA and protein molecules exist in knotted form, previously it has not been possible to tie a molecule into more than one complex knot.

The new research published today in journal , demonstrates how the scientists were able to mimic natural molecular biological processes to achieve lab-made alternatives for a range of potential applications. Biology uses ‘molecular assistants’ called chaperones to fold proteins into knotted structures and the 91ֱ�� scientists applied the same concept to a synthetic molecular strand using metal atoms to guide the folding process.

Professor David Leigh, from The University of Manchester led the research, he said: “We were able to tie different knots in a molecular strand by using metal atoms to fold and entwine the strand. The two green sites bind to a copper atom; the three purple sites bind to a lutetium atom. Joining the end groups prevents the knot untying when the metal atoms are removed.”

The same group had previously tied the world’s tiniest knot and now progressed their research here by using basic methods which would be familiar to anyone who joined the Scouts. Being able to make different types of molecular knots means that scientists should be able to probe how knotting affects strength and elasticity of materials which will enable them to weave polymer strands to generate new types of materials.

The key was to intersperse binding sites for different metal ions along the molecular strand. When a metal atom binds to specific sites on the strand it causes the strand to fold creating an over-under ‘tangle’ in the thread. Different tangles combine to form larger knots according to tangle theory (developed by mathematician John H. Conway, also known for developing ‘Game of Life’). Different combinations of metal ions (copper and/or Lutetium, or none, allowed any one of three different knots—an unknot, a trefoil knot, and a three-twist knot—to be tied in the same molecular strand.

Tying the molecular strand into different knots changes its properties. When the strand is tied into the tightest, most complex, knot – the three-twist knot – it can bind two metal atoms simultaneously, one copper atom and one lutetium atom. However, the looser knots (e.g. the trefoil knot and the unknot) can only bind one metal atom at a time – either one copper atom, or one lutetium atom. Unexpectedly, the metal binding can also change the way the knotted loop is entangled, like a molecular game of cat’s cradle.

The ability to tie a molecular strand into different knots, and subsequently change the region and degree of entanglement, opens up new opportunities and research directions for modifying the function and properties of other molecular chains, such as polymers and plastics.

The online events took place throughout the week commencing Monday, 27 July as part of wider celebrations across The University of Manchester. They provided an opportunity for both staff and students to mark summer graduation after physical ceremonies were postponed due to the ongoing COVID-19 pandemic.

A total of 12 FSE graduations were spread over the week, with events held for mathematics; mechanical, aerospace and civil engineering; physics and astronomy; electrical and electronic engineering; fashion business and technology; materials science and engineering; chemical engineering and analytical science; earth and environmental sciences; computer science; and chemistry.

The move online meant students were able to celebrate despite being situated all across the globe. It showed that while they may not be in the city at the moment, 91ֱ�� is behind its graduates as they take their next steps out into the world.

Each subject area celebrated in its own unique way - as shown in the recorded videos below:

School of Engineering

School of Natural Sciences

A huge congratulations to all of our FSE graduates, and the best of luck for the future!

This is why we're doing our very best to keep you updated in the lead-up to the new academic year. As such, we'll be answering your questions in a series of video updates.

In this first video, Education Officer in the Students' Union Chloe Salin speaks to the Heads of Education for our Faculty's two Schools – Professor Peter Green in the School of Engineering and Professor Andrew Horn in the School of Natural Sciences – about their plans for a new-look teaching and learning experience.

You'll hear all about the benefits of blended learning; safety on campus; being part of the 91ֱ�� community (and student societies); lab, field and group work; exams and assessment; accessing software; and remote learning.

It's a lot to cover, but we hope the video will help to reassure you that this year's university experience will be what you expect from a university ranked 27^th in the world for two years running.

Please bear in mind that this is what we know right now. We'll provide more information, as and when we have it, in the videos to come.

If you have any questions you would like to ask, please send them through to your Department Admissions or Student Experience Team. They will then be either answered directly, or in one of the upcoming videos.

91ֱ�� is the most targeted university for graduate employers, and last week's announcement of new post-study work visas will be welcomed by many international students hoping to further their studies at the University.

It was confirmed that post-work study visas will be extended for up to three years post-graduation for international PhD graduates, and that international undergraduate and postgraduate-taught students will be able to live and work in the UK for up to two years post-graduation.

The new Graduate Route is to launch in the summer of 2021, meaning any eligible student who graduates next summer or after will be able to apply, including students who have already started their courses.

As well as being the most targeted university for graduate employers, The University of Manchester has a team specifically dedicated to helping postgraduate students further their careers.

Find out more about the new Graduate Route and post-study work visa extensions on the .

The academics from across the University’s Faculty of Science and Engineering (FSE) have been awarded for pioneering research advances within their respective fields, which range from inorganic chemistry to two-dimensional materials.

The Royal Society of Chemistry’s Prizes and Awards are awarded in recognition of originality and impact of research, or for each winner’s contribution to the chemical sciences industry or education. They also acknowledge the importance of teamwork across the chemical sciences, as well as the abilities of individuals to develop successful collaborations.

Full list of RSC Prize Winners:

• Dr Anthony Green -
• Dr Jordi Bures -
• Dr Radha Boya -
• Dr Sihai Yang -
• Professor Cinzia Casiraghi -
• Professor David Procter -
• Professor Martin Schröder -
• Professor Sabine Flitsch -
• Professor Stephen Liddle -
• Professor Vernon Gibson -
• Professor Nik Kaltsoyannis - 

Professor Martin Schröder, Vice President and Dean for FSE, has been named the winner of the Royal Society of Chemistry’s Nyholm Prize for Inorganic Chemistry. Dr Schröder won the award for seminal work on the design, synthesis and characterisation of porous metal-organic framework materials for substrate binding and selectivity.

After receiving the award, Professor Schröder said: “I am deeply honoured to be awarded the 2020 Nyholm Prize for Inorganic Chemistry from the Royal Society of Chemistry. This is a wonderful testament to the many undergraduate and PhD students, postdoctoral researchers and the national and international collaborators from industry, academia and at national facilities that have contributed so much to this research programme over many years. A huge thank you to all of them.

“The list of previous winners reads like a Who’s Who of inorganic chemistry over the years, with the very first winner in 1974/75 being Jack Lewis, who was my postdoctoral mentor, and in 2001/2 Jon McCleverty, who was my undergraduate tutor. We all stand on the shoulders of others.”

Of the previous winners of Royal Society of Chemistry Awards, an illustrious list of 50 have gone on to win Nobel Prizes for their pioneering work, including 2016 Nobel laureates Jean-Pierre Sauvage, Fraser Stoddart and Ben Feringa.

The that make up the University’s Faculty of Science and Engineering all have a strong reputation for teaching and learning, and for producing employable graduates. The programmes are designed to provide flexibility of choice and are continually revised to reflect new development in each subject area allowing students and academics to work at the cutting edge of science.