The five-year multi-centre research project ā€“ supported by Ā£10mn funding from Wellcome ā€“ involves researchers from the Universities of Cambridge, Kent, Ā鶹“«Ć½, Oxford, and Imperial College London. SynHG is led by Professor Jason Chin of the MRC Laboratory of Molecular Biology; he was also recently announced as the founding Director of the Generative Biology Institute at the Ellison Institute of Technology, Oxford, and a Professor at the University of Oxford.

A dedicated social science programme, led by Professor Joy Zhang of the Centre for Global Science and Epistemic Justice at the University of Kent, runs throughout the project alongside the scientific development. The programme will work with civil society partners around the world to actively explore, assess and respond to the socio-ethical implications of tools and technologies developed by SynHG.

The benefits of human genome synthesis to research and beyond 
Since the completion of the Human Genome Project at the start of the century, researchers have sought the ability to write our genome from scratch. Unlike genome editing, genome synthesis allows for changes at a greater scale and density, with more accuracy and efficiency, and will lead to the determination of causal relationships between the organisation of the human genome and how our body functions. Synthetic genomes have the potential to open up brand new areas of research in creating targeted cell-based therapies, virus-resistant tissue transplantation and extensions may even enable the engineering of plant species with new properties, including the ability to withstand harsh climate. 

To date, scientists have successfully developed synthetic genomes for microbes such as E. coli. The field of synthetic genomics has accelerated in recent times, and advances in machine learning, data science and AI showing promise, with synthesised DNA becoming more widely available. However, todayā€™s technology is not able to produce large, more complex sections of genetic material, such as found in crops, animals and humans. 

The research team are focusing on developing the tools and technology to synthesise large genomes exemplified by the human genome. Focusing on the human genome, as opposed to other model organisms such as mice, will allow researchers to more quickly make transformative discoveries in human biology and health.

 Professor Jason Chin, Founding Director of the Generative Biology Institute at EIT, Oxford, said: ā€œThe ability to synthesize large genomes, including genomes for human cells, may transform our understanding of genome biology and profoundly alter the horizons of biotechnology and medicine. With SynHG we are building the tools to make large genome synthesis a reality, and at the same time we are pro-actively engaging in the social, ethical, economic and policy questions that may arise as the tools and technologies advance.  We hope that Wellcomeā€™s support for this combination of approaches will help facilitate substantive societal benefit.ā€

A bold, ambitious project facing complex scientific challenges 
SynHG focuses on developing the foundational tools and methods required to equip more researchers in the future. This research journey will potentially catalyse new technologies in the field of engineering biology, generating exciting discoveries about how cells use their genomes even before achieving complete genome synthesis. 

The team of researchers hope to provide proof of concept for large genome synthesis by creating a fully synthetic human chromosome, which makes up approximately 2% of our total DNA. Initially, the team hope to establish methods where small changes are made to the sequence of a chromosome with minimal onward effect on the proteins that it produces. 

Setting the foundation ā€“ testing the concept, iterating the methods, and embedding ethical considerations ā€“ could alone take many years. Even as engineering biology technologies improve, reliably building a complete synthetic human genome and meaningfully applying it to human health will likely take decades.

Michael Dunn, Director of Discovery Research at Wellcome, said: ā€œOur DNA determines who we are and how our bodies work and with recent technological advances, the SynHG project is at the forefront of one of the most exciting areas of scientific research. Through creating the necessary tools and methods to synthesise a human genome we will answer questions about our health and disease that we cannot even anticipate yet, in turn transforming our understanding of life and wellbeing.ā€ 

Professor Patrick Yizhi Cai, Chair of Synthetic Genomics at the University of Ā鶹“«Ć½ said: "We are leveraging cutting-edge generative AI and advanced robotic assembly technologies to revolutionize synthetic mammalian chromosome engineering. Our innovative approach aims to develop transformative solutions for the pressing societal challenges of our time, creating a more sustainable and healthier future for all."

Embedding global socio-ethical discussions in scientific advancements 
To effectively translate scientific ambition into meaningful and potentially profound societal benefits, it is essential that there is proactive and sustained engagement with the evolving socio-ethical priorities and concerns of diverse communities. 

Wellcome is also funding Care-full Synthesis, a dedicated social research initiative conducting empirical studies with diverse publics worldwide. Led by Professor Joy Y. Zhang and hosted by the Centre for Global Science and Epistemic Justice (GSEJ) at the University of Kent, the project builds on GSEJā€™s global network of academic, civil society, industry and policy partners to promote a new approach of scienceā€“society dialogue that is Open, Deliberative, Enabling, Sensible & Sensitive, and Innovative (ā€˜ODESSIā€™). 

Professor Joy Zhang, Founding Director of the GSEJ at the University of Kent said: ā€œWith Care-full Synthesis, through empirical studies across Europe, Asia-Pacific, Africa, and the Americas, we aim to establish a new paradigm for accountable scientific and innovative practices in the global ageā€”one that explores the full potential of synthesising technical possibilities and diverse socio-ethical perspectives with care.ā€ 

Over the next five years, the team will undertake a transdisciplinary and transcultural investigation into the socio-ethical, economic, and policy implications of synthesising human genomes. The project places particular emphasis on fostering inclusivity within and across nation-states, while engaging emerging publicā€“private partnerships and new interest groups. 

Through the generation of rich empirical data, the team will develop a toolkit to enable effective integration of careful thinking into the management, communication, and delivery of human genome synthesis. This work aims to substantially expand the practice of accountable science and innovation, reflecting the complex realities of a hyperconnected yet ideologically fragmented world. Care-full Synthesis will achieve this by advancing a fresh approach to engaging with global communities, ensuring that fast-moving science is accompanied by robust social and legal deliberation, and identifying innovative strategies to co-ordinate regional and global governance accounting for diverse social priorities and scientific pathways.

In a boon for the future of data storage technologies, the researchers have made a new single-molecule magnet that retains its magnetic memory up to 100 Kelvin (-173 Ā°C) ā€“ around the temperature of the Moon at night.

The finding, published in the journal , is a significant advance on the previous record of 80 Kelvin (-193 Ā°C). While still a long way from working in a standard freezer, or at room temperature, data storage at 100 Kelvin could be feasible in huge data centres, such as those used by Google.

If perfected, these single-molecule magnets could pack vast amounts of information into incredibly small spaces ā€“ possibly more than three terabytes of data per square centimetre. Thatā€™s around half a million TikTok videos squeezed into a hard drive thatā€™s the size of a postage stamp.

The research was led by Ā鶹“«Ć½, with computational modelling led by the Australian National University (ANU).

David Mills, Professor of Inorganic Chemistry at Ā鶹“«Ć½, said: ā€œThis research showcases the power of chemists to deliberately design and build molecules with targeted properties. The results are an exciting prospect for the use of single-molecule magnets in data storage media that is 100 times more dense than the absolute limit of current technologies.

ā€œAlthough the new magnet still needs cooling far below room temperature, it is now well above the temperature of liquid nitrogen (77 Kelvin), which is a readily available coolant. So, while we wonā€™t be seeing this type of data storage in our mobile phones for a while, it does make storing information in huge data centres more feasible.ā€

Magnetic materials have long played an important role in data storage technologies. Currently, hard drives store data by magnetising tiny regions made up of many atoms all working together to retain memory. Single-molecule magnets can store information individually and donā€™t need help from any neighbouring atoms to retain their memory, offering the potential for incredibly high data density. But, until now, the challenge has always been the incredibly cold temperatures needed in order for them to function.

The key to the new magnetsā€™ success is its unique structure, with the element dysprosium located between two nitrogen atoms. These three atoms are arranged almost in a straight line ā€“ a configuration predicted to boost magnetic performance but realised now for the first time.

Usually, when dysprosium is bonded to only two nitrogen atoms it tends to form molecules with more bent or irregular shapes. In the new molecule, the researchers added a chemical group called an alkene that acts like a molecular pin, binding to dysprosium to hold the structure in place.

The team at the Australian National University developed a new theoretical model to simulate the moleculeā€™s magnetic behaviour to allow them to explain why this particular molecular magnet performs so well compared to previous designs.

Now, the researchers will use these results as a blueprint to guide the design of even better molecular magnets.

has been selected to receive the Robert Robinson Prize, while is one of this year's three Tilden Prize recipients.

Professor Larrosa and Professor Barran are among the more than 40 Research and Innovation Prize winners, which recognises researchers who have displayed their brilliance when it comes to research and innovation.

and have earned the Technical Excellence Prize for their outstanding dedication and technical expertise in running the at Ā鶹“«Ć½. The prize recognises outstanding contributions to the chemical sciences made by individuals or teams working as technicians or in technical roles. 

Prof Larrosa won his prize for contributions to organic chemistry in the area of ruthenium-catalysed Cā€“C bond formation, and receives Ā£3,000 and a medal.

His investigates the development of catalytic processes that enable chemists in industry and academia to synthesise valuable molecules in a more straightforward and sustainable fashion. The main approach in the group involves the application of analytical tools to the detailed study of the modes of operation of transition metal catalysts, and then using this new knowledge to develop more powerful and efficient catalysts.

After receiving the prize, Prof Larrosa said: ā€œIt is such an honour to receive the Robert Robinson Award, especially given its history of celebrating transformative contributions to organic chemistry. This recognition reflects the creativity, persistence and collaborative spirit of the brilliant researchers I have had the privilege to work with over the years. I am proud of what we have achieved together, and deeply grateful for the support of my colleagues, mentors and the wider scientific community.ā€

Professor Barran was recognised with the Tilden Prize for her work on the application of ion mobility mass spectrometry to complex biological systems, and breakthroughs in biomarker discovery ā€“ notably non-invasive sampling to diagnose Parkinson's disease.

Her focuses on developing advanced mass spectrometry techniques to study the structure and behaviour of proteins and other biomolecules, with applications in understanding the fundamentals of biology, the mechanistic reasons for diseases and the development of therapeutics and diagnostics. One of our most notable achievements is the collaborative work with Joy Milne, a retired nurse who possesses an extraordinary sense of smell and noticed a distinct odour associated with Parkinsonā€™s disease.

This observation led to research demonstrating that sebum, an oily substance secreted by the skin, contains compounds that can serve as biomarkers for Parkinsonā€™s. Using mass spectrometry, our team identified specific molecules in sebum that differ between individuals with and without Parkinsonā€™s disease. This discovery has paved the way for the development of a non-invasively sampled and rapid diagnostic test that can detect Parkinsonā€™s disease with high accuracy, potentially allowing for earlier intervention and treatment.

Prof Barran won Ā£5,000 and a medal. 

After receiving the prize, Prof Barran said: ā€œI was absolutely thrilled! This prize was formally won by both my PhD advisors, Harry Kroto and Tony Stace, my undergraduate personal tutor, Dave Garner, and many other brilliant scientists. I felt totally honoured to be among these people who I have always respected. In my case, I attribute winning to the people that I have been privileged to work with. I noted that out of about 200 recipients I was the ninth female. This also made me feel pretty pleased!ā€

Dr Muralidharan Shanmugam and Adam Brookfield are two EPSRC National Research Facility (NRF) for Electron Paramagnetic Resonance Spectroscopy technical specialists named as the winners of one of the Royal Society of Chemistryā€™s team prizes, which celebrate discoveries and innovations that push the boundaries of science.

The duo have been recognised for their outstanding dedication and technical expertise in running the facility at Ā鶹“«Ć½. Electron paramagnetic resonance (EPR) is the spectroscopic technique that is selective and sensitive to unpaired electrons. The unpaired electrons could be intrinsic to the materials studied or could be induced via a process (e.g light/heat/chemically) to provide information on structure, kinetics and much more, with applications covering all areas of physics, chemistry, biology and materials science. The technical team at the EPSRC NRF both maintain the equipment and assist users with the design, implementation and analysis of proposed experiments.

They will share Ā£3,000 and receive a trophy.

 After receiving the prize, Adam Brookfield said: ā€œBoth Murali and I are over the moon that our contributions have been recognised by the RSC with this award.

"We're both nosey scientists at heart, we want to provide the best instrument access and knowledge to our users to enable their world-class science. We're in a unique position where we get to see and adapt the facility to the trends and hotspots in research areas, alongside training the next generation of scientific leaders.ā€

The Royal Society of Chemistryā€™s prizes have recognised excellence in the chemical sciences for more than 150 years. This yearā€™s winners join a prestigious list of past recipients in the RSCā€™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.

Dr Helen Pain, Chief Executive of the Royal Society of Chemistry, said: ā€œThe 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 worldā€™s most pressing challenges.

ā€œOur 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 RSCā€™s work as volunteers. We celebrate winners from both industry and academia, as well as individuals, teams, and the science itself.

ā€œTheir passion, dedication and brilliance are an inspiration. I extend my warmest congratulations to them all.ā€

For more information about the RSCā€™s prizes portfolio, visit .

Enzymes are proteins that catalyse chemical reactions, turning one substance into another. In labs, scientists engineer these enzymes to perform specific tasks like the sustainable creation of medicines, and materials. These biocatalysts have many environmental benefits as they often produce higher product quality, lower manufacturing cost, and less waste and reduced energy consumption. But to find ā€˜the oneā€™, scientists must test hundreds of variants for their effectiveness, which is a slow, expensive, and resource-intensive process.

Research conducted by Ā鶹“«Ć½ in collaboration with AstraZeneca is changing this. The team developed a method for a technique that can test enzyme activity up to 1,000 times faster than traditional methods. The new method, developed over the last eight years and detailed today in the journal  is called DiBT-MS (Direct Analysis of Biotransformations with Mass Spectrometry).

It builds on an existing technology called DESI-MS (Desorption Electrospray Ionization Mass Spectrometry), a powerful tool that allows scientists to analyse complex biological samples without the need for extensive sample preparation. 

By making small adaptations to the technology, the scientists designed a protocol to directly analyse enzyme-triggered chemical reactions, known as biotransformations, in just minutes. The new method can process 96 samples in just two hoursā€”tasks that would previously take days using older techniques.

It has also been optimised to allow the researchers to reuse sample slides multiple times improving testing efficiency and decreasing the use of solvents and plasticware.

The team has already successfully applied this technique to a range of enzyme-driven reactions, including those enzymes particularly valuable in the development of therapeutics.

Looking ahead, Ā鶹“«Ć½ will continue to explore ways to boost partnerships between laboratories and tackle other challenges that often hinder collaboration, such as geographical barriers and limited funding.

This research was partly funded by a UKRI Prosperity Partnership grant in collaboration with AstraZeneca.

Journal: Nature Protocols

Full title: Direct analysis of biotransformations with mass spectrometryā€”DiBT-MS

DOI: 10.1038/s41596-025-01161-9

Link:

Water pollution is one of the growing challenges of modern life. Many everyday items, from medications to cosmetics, leave behind residues that donā€™t fully break down after use. These pollutants often find their way into water systems, where they disrupt ecosystems and cause harm to plants, animals and humans.

The research, published in the journal ,  describes a new method using a molecular structure called a metal-organic cage (MOC). These tiny cages act like traps designed to catch and hold harmful molecules commonly found in our water supplies.

While MOCs have been studied before for gas and chemical capture, they are most commonly studied in chemical solvents where their performance differs significantly from that observed in water. Being able to demonstrate capture of established wastewater pollutants in water is thus a step towards the application of these cages for real-world applications.

Jack Wright, a Researcher at Ā鶹“«Ć½, who completed the research as part of his PhD, said: ā€œBeing able to use MOCs in water is a really exciting development. We know how valuable MOCs are for capturing unwanted substances, but until now researchers have not been able to apply them to real-world water systems.

ā€œMany harmful chemicals are difficult to remove from water, and with water pollution becoming a global crisis, this new MOC technology could provide a valuable tool to help clean up water systems and prevent pollutants from entering our ecosystem, particularly in rivers and lakes near urban or industrial areas where wastewater discharge is most common.ā€

The cages are made up of metal ions connected by organic molecules, forming a hollow pyramid-like structure. These hollow spaces at the centre of these structures are where the MOCs trap specific molecules, like pollutants or gases.

The new structure incorporates chemical groups called sulfonates to make it compatible with water, allowing it to function in real-world water systems, like rivers or wastewater.

It uses a natural effect called hydrophobic binding, where contaminant molecules preferentially ā€œstickā€ to the inside of the cage rather than staying in the water. This allows the material to selectively capture and hold pollutants, even in challenging water environments.

Dr Imogen Riddell, PhD supervisor and researcher at Ā鶹“«Ć½, said: ā€œOne of the real strengths of this method is its flexibility. The approach we have developed could be used to design other water-soluble MOCs with different sizes or properties. This opens the door to many future applications, including cleaning up different kinds of pollutants, development of green catalysts or even development of drug delivery strategies .ā€

Now, the researchers will look to further expand the water-soluble cages, to enable capture of more, different contaminants, and are working  towards the development of robust routes to recycling the cages to support their development as sustainable water purification aids.

Just like the proteins in our muscles, which convert chemical energy into power to allow us to perform daily tasks, these tiny rotary motors use chemical energy to generate force, store energy, and perform tasks in a similar way.

The finding, from Ā鶹“«Ć½ and the University of Strasbourg, published in the journal provides new insights into the fundamental processes that drive life at the molecular level and could open doors for applications in medicine, energy storage, and nanotechnology.

The artificial rotary motors are incredibly tinyā€”much smaller than a strand of human hair. They are embedded into polymer chains of a synthetic gel and when fuelled, they work like miniature car engines, converting the fuel into waste products, while using the energy to rotate the motor.

The rotation twists the gelā€™s molecular chains, causing the gel to shrink, storing the energy, much like winding like an elastic band. The stored energy can then be released to perform tasks.

So far, the scientists have demonstrated the motorā€™s ability to open and close micron-sized holes and speed up chemical reactions.

Professor Leigh added: ā€œMimicking the chemical energy-powered systems found in nature not only helps our understanding of life but could open the door to revolutionary advances in medicine, energy and nanotechnology.ā€

The extinction of the Dinosaur was a tumultuous time that included some of the largest volcanic eruptions in Earthā€™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 Earthā€™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 ā€“ led by Ā鶹“«Ć½ ā€“ 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 COā‚‚ emissions caused a slow warming of about 3Ā°C across this period. There was also a short cold ā€œsnapā€ ā€” cooling of about 5Ā°C ā€” 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 werenā€™t catastrophic enough to kill them off dinosaurs.

Dr Lauren Oā€™Connor, lead scientist and now Research Fellow at Utrecht University, said: ā€œThese 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.ā€

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: ā€œThe 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.ā€

Bart van Dongen, Professor of Organic Geochemistry at Ā鶹“«Ć½, added: ā€œThis 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.ā€

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

A group of leading international scientists is calling for a global conversation about the potential creation of "mirror bacteria"ā€”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 Ā鶹“«Ć½, 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: ā€œWhile mirror bacteria are still a theoretical concept and something that we likely wonā€™t see for a few decades, we have an opportunity here to consider and pre-empt risks before they arise.

ā€œThese 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: ā€œAt this stage, itā€™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 Ā鶹“«Ć½ in autumn 2025.ā€

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 bodyā€™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 ā€“ Escherichia coli ā€“ 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 skinā€™s surface, potentially enhancing the precision of an artificial limb.

The Ā鶹“«Ć½ iGEM team were Damian Ungureanu, Devika Shenoy, Francisco Correia, Janet Xu, Jia Run Dong, Usrat Nubah, Yuliia Anisimova, and Zainab Atique-Ur-Rehman.

, said: ā€œIā€™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: ā€œI have supervised the Ā鶹“«Ć½ iGEM teams together with Professor Rainer Breitling since 2013.

ā€œOur 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.

ā€œIn 2016, the team also scooped the special award for ā€˜Best Computational Modelā€™ and were shortlisted for the ā€˜Best Education and Public Engagementā€™ award.ā€

This yearā€™s Ā鶹“«Ć½ 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: ā€œWorking 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.ā€

Devika Shenoy, second year Biomedical Sciences student, said: ā€œI 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.ā€

Biocatalysis is a process that uses enzymes as natural catalysts to carry out chemical reactions. Scientists at Ā鶹“«Ć½ 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" ā€” a sequence of enzyme-driven reactions ā€” 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 Ā鶹“«Ć½, 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 ā€“ known as MIL-125 ā€“ 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 materialā€™s efficiency, enabling it to capture benzene even at ultra-low concentrations ā€“ measured at parts per million (ppm) ā€“ a significant improvement over current materials.

The new material ā€“ now known as MIL-125-Zn ā€“ 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 Ā鶹“«Ć½ Institute of Biotechnology at Ā鶹“«Ć½, added: ā€œMy team has spent more than a decade studying how ice-binding proteins, found in polar fish, can interact with ice crystals, and weā€™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.ā€

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 whatā€™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 Ā鶹“«Ć½ 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 ā€˜capturingā€™ the pathogens or their toxins.

, a researcher from at Ā鶹“«Ć½, said ā€œDuring the Covid-19 pandemic, our team introduced the first lateral flow tests which used sugars instead of antibodies as the ā€˜recognition unitā€™. 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.ā€

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 ā€œGlycans 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.ā€

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 Ā鶹“«Ć½ Institute of Biotechnology at Ā鶹“«Ć½, said ā€œOne 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.ā€

They found that some of the sugars they prepared could be used to detect the cholera toxin ā€“ a harmful protein produced by bacteria ā€“ 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: ā€œWe 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.ā€

The study provides evidence that the artificial ā€œfluoro-sugarsā€ 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 Ā鶹“«Ć½, 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 Ā鶹“«Ć½, Glasgow and Warwick, have designed a hydrogel ā€“ a material mostly made of water ā€“ that stabilises proteins, protecting its properties and functionality at temperatures as high as 50Ā°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 ā€“ called excipients ā€“ 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 paperā€™s corresponding authors. He said: ā€œIn 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 peopleā€™s arms quickly after thawing.  

ā€œThe technology weā€™ve developed marks a significant advance in overcoming the challenges of the existing ā€˜cold chainā€™ which delivers therapeutic proteins to patients. The results of our tests have very encouraging results, going far beyond current hydrogel storage techniquesā€™ 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.ā€

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 ā€“ the process which limits or prevents their effectiveness as medicines.

The unique mechanical properties of the gelā€™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 25Ā°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 50Ā°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 teamā€™s analysis showed that the gelsā€™ structures remained intact and the proteins had been entirely prevented from aggregating.

is the paperā€™s other corresponding author. He said: ā€œDelivering 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.ā€

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 teamā€™s paper, titled ā€˜Mechanical release of homogenous proteins from supramolecular gelsā€™, is published in Nature.

The research was supported by funding from the European Unionā€™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 , Ā鶹“«Ć½ scientists have discovered a new family of ligase enzymes ā€“ 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 Ā鶹“«Ć½ 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, ā€œThe 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.ā€

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 Chemistryā€™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 Ā£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 Ā鶹“«Ć½.

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 ā€“ the ones in our laptops ā€“ 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: ā€œItā€™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.ā€

has been named winner of the Royal Society of Chemistryā€™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 Ā£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 natureā€™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: ā€œIā€™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.ā€

has been named winner of the Royal Society of Chemistryā€™s Harrison-Meldola Prize.

Dr Lovelock won the prize for the development of innovative biocatalytic approaches to produce therapeutic oligonucleotides. She also receives Ā£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 Lovelockā€™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 (natureā€™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: ā€œI 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.ā€

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

The team is a collaboration between Ā鶹“«Ć½, 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 MOFā€™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 Schrƶder, Vice President and Dean, Faculty of Science and Engineering, who leads the group at Ā鶹“«Ć½, said: ā€œI 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.ā€

The Royal Society of Chemistryā€™s prizes have recognised excellence in the chemical sciences for more than 150 years. This yearā€™s winners join a prestigious list of past winners in the RSCā€™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: ā€œThe 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 worldā€™s most pressing challenges.

ā€œOur 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 RSCā€™s work as volunteers. We celebrate winners from both industry and academia, as well as individuals, teams, and the science itself.

ā€œTheir passion, dedication and brilliance are an inspiration. I extend my warmest congratulations to them all.ā€

For more information about the RSCā€™s prizes portfolio, visit .

The centre has been awarded Ā£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; ā€œAccurately 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.ā€™ā€™

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 Ā£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 Ā鶹“«Ć½, 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 companyā€™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 Lubrizolā€™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 Ā£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 ā€“ a platinum group metal ā€“ 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 Ā鶹“«Ć½ 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 catalystā€™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: ā€œCatalysis 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.ā€

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 Ā£49.35m from the UKRI Infrastructure Fund to establish C-MASS - a national hub-and-spoke infrastructure designed to integrate and advance the countryā€™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 Ā鶹“«Ć½ 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.

Ā鶹“«Ć½ is renowned for its expertise in mass spectrometry. J.J. Thomson, who was an alumnus of Ā鶹“«Ć½, 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 Ā鶹“«Ć½ 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 Ā鶹“«Ć½ 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 Huntingtonā€™s disease and rheumatic heart disease, diagnosing Parkinsonā€™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. 

Ā鶹“«Ć½ 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 Ā鶹“«Ć½ 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 Ā鶹“«Ć½ 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: ā€œEngineering biology has the power to transform our health and environment, from developing life-saving medicines to protecting our environment and food supply and beyond.

ā€œOur latest Ā£100m investment through the UKRI Technology Missions Fund will unlock projects as diverse as developing vaccinesā€¦preventing food waste through disease resistant crops, reducing plastic pollution, and even driving efforts to treat snakebites.

ā€œWith 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.ā€

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.  Ā鶹“«Ć½ has a broad range of expertise in engineering biology across its three Faculties and is also home to the international centre of excellence, the Ā鶹“«Ć½ 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 ā€“ a small molecule that binds with the DD degron ā€“ 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: ā€œSafety 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.ā€

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 ā€œsuicideā€ 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 ā€œsuicideā€ 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 Ā£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 yearā€™s Laureates were selected by an independent jury of expert scientists from across the UK.

Professor Anthony Green, a Lecturer in Organic Chemistry from Ā鶹“«Ć½, 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 Ā鶹“«Ć½, 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: ā€œProviding recognition and funding early in a scientistā€™s career can make the difference between discoveries that remain in the lab and those that make transformative scientific breakthroughs.

ā€œWe 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.ā€

, President and CEO of The New York Academy of Sciences and Chair of the Awardsā€™ Scientific Advisory Council, added: ā€œFrom 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 yearā€™s Laureates and Finalists are pushing the boundaries of science and working to make the world a better place. Thank you to this yearā€™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.ā€

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 donā€™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 Ā鶹“«Ć½ 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: ā€œShell aims to transition to a net-zero emissions energy business by 2050 and our work with the Ā鶹“«Ć½ 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.ā€

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

ā€œOur 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.

ā€œMore than Ā£17m of Government funding is backing vital projects including work in Belfast to unearth life-saving drugs, in Ā鶹“«Ć½ to improve skin health research and in Cambridge to tackle a major source of global pollution ā€“ enhancing the health and wellbeing of people across our country and beyond.ā€

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

ā€œThe 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 Ā£17 million in ten projects.

ā€œThis 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 Ā£21 million into research and development.

ā€œThe 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.ā€

Industrial biotechnology uses natureā€™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 ā€“ a process that speeds up chemical reactions ā€“ 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 worldā€™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 Ā鶹“«Ć½ 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 Luminspheresā„¢-tracers under reservoir conditions in a laboratory setting.  Phase-II of the programme will validate multicoloured Luminspheresā„¢ tracers under flow conditions.

Chromitionā€™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, Chromitionā€™s Chief Executive, said: ā€œShellā€™s continued commitment is a testament to the progress achieved to date in developing Chromitionā€™s in-line tracer detection system, which for the first time will enable remote, real-time reservoir surveillance to improve the management of subsurface resourcesā€.

Veronica Simmonds, Commercial Innovation Partnerships Manager/GameChanger, Shell, added: ā€œWe 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 usā€.

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 Ā鶹“«Ć½, 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 Ā鶹“«Ć½ Institute of Biotechnology and the Department of Chemistry at Ā鶹“«Ć½, said: ā€œOur 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.  

ā€œOur 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.ā€  

If adopted in industry, the Enzyme Discovery teamā€™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 Ā鶹“«Ć½, 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 ā€“ which brought together minds with specialities in areas such as the physics of information and molecular biology ā€“ join a prestigious list of past winners in the RSCā€™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 Ā鶹“«Ć½, said: ā€œItā€™s been fantastic to be part of such a talented team on the Molecular Ratcheteers project, and weā€™re proud to have developed concepts that could truly drive forward engineering in the nanoworld.ā€ 

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 todayā€™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: ā€œThe 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.  

ā€œThe 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.ā€ 

The Royal Society of Chemistryā€™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 Chemistryā€™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.

ā€œThe 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,ā€ says Professor Martin Schrƶder, lead author of the paper which is published in . ā€œBecause of the small difference in their boiling points (just 0.6 ā„ƒ) the separation of benzene and cyclohexane is currently extremely difficult and expensive to achieve via distillation or other methodsā€.

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.

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

The grant will begin the transformation of the Universityā€™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.

Ā鶹“«Ć½ is the birthplace of Chemical Engineering, and the University continues to be a prime destination for industryā€relevant training. Today our academic researchers are at the forefront of some of the globeā€™s most transformational science and engineering discoveries.

Professor Lev Sarkisov, Head of the Department of Chemical Engineering has said about the project: ā€œWe 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, Ā鶹“«Ć½ will lead research and innovation on clean energy working closely with industry and delivering a new curriculum for the next generation chemical engineers.ā€

The new Industrial Hub for Sustainable Chemical Engineering will be developed in the James Chadwick Building, which is part of the new Ā£450m home for engineering and materials science - Ā鶹“«Ć½ Engineering Campus Development (MECD) - opening in September 2022.

Professor Dame Nancy Rothwell, President and Vice-Chancellor of Ā鶹“«Ć½, has said: ā€œWith support from the Wolfson Foundation, Ā鶹“«Ć½ will be able to significantly accelerate the UKā€™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.ā€

About the new home for engineering and materials science

Ā鶹“«Ć½ā€™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 Ā鶹“«Ć½, 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 worldā€™s carbon emissions.

Professor Sarah Haigh has been named winner of the Royal Society of Chemistryā€™s Analytical Division mid-career Award. Based at the University of Ā鶹“«Ć½, 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: ā€œIā€™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.ā€

Most science and engineering processes occur in liquids or gases. Professor Haighā€™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 Chemistryā€™s Interdisciplinary Prize. Based at the University of Ā鶹“«Ć½, 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: ā€œI 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.ā€

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 Micklefieldā€™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 Chemistryā€™s Tilden Prize. Based at the University of Ā鶹“«Ć½, 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: ā€œI was delighted and honoured but surprised.ā€

Professor Hardacreā€™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: ā€œGreat science changes the way we think about things ā€“ 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. 

ā€œAlthough 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 Ā鶹“«Ć½ is a fantastic example of why we celebrate great science, and weā€™re very proud to recognise their contribution today.ā€

Reported in the journal, , a group of researchers from The University Ā鶹“«Ć½, 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 Ā鶹“«Ć½, coordinated the research. He said: ā€œIt 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 researcherā€™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, ā€˜A terminal neptunium(V)ā€“mono(oxo) complexā€™, 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 Ā鶹“«Ć½ 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 Ā鶹“«Ć½ 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 Ā鶹“«Ć½ 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, Ā鶹“«Ć½ 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.”

Ā鶹“«Ć½ 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 Ā鶹“«Ć½ nearly 20 years ago, are at the forefront of research into efficient gas separations. Graphene, first isolated by physicists at Ā鶹“«Ć½ 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 Ā鶹“«Ć½ 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 Ā鶹“«Ć½ 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 Ā鶹“«Ć½; 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 Ā鶹“«Ć½ 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 Ā鶹“«Ć½, 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 Ā鶹“«Ć½.

David Leys, group leader at the Ā鶹“«Ć½ Institute of Biotechnology of Ā鶹“«Ć½, says: ā€œOur 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.ā€

Marc Delcourt, co-founder and CEO of Global Bioenergies, adds: ā€œNature 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.ā€

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 Ā鶹“«Ć½ 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 Ā鶹“«Ć½ 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 Ā鶹“«Ć½, 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 Ā鶹“«Ć½ā€™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.