Professor Bruce Turnbull - 2024 Bader Prize winner

Professor Bruce Turnbull CChem FRSC

Winner: 2024 Bader Prize

University of Leeds

For the development and application of bioorthogonal approaches in engineering functional protein and carbohydrate based systems.

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We know enough about chemistry itself that the most exciting discoveries and developments are going to come at the interface with other subjects.

The surface of every living cell is covered in a layer of complex carbohydrate structures known as the glycocalyx. The types of carbohydrates present differ from one cell type to another and can also change when healthy cells become cancerous. The glycocalyx is like a forest with long polysaccharides forming the forest’s canopy. This canopy sits above smaller tree-like glycoproteins and glycolipids – like the forest floor – which are embedded in the cell membrane. Anything approaching the cell membrane must travel through this carbohydrate forest.

Professor Turnbull’s group is interested in understanding how proteins interact with the carbohydrates of the glycocalyx ‘forest’. They are investigating methods to re-engineer the carbohydrate-binding proteins and the sugars they recognise for applications in diagnosing disease and targeting drugs to specific cell types.

Read winner biography

Bruce Turnbull grew up on a farm in the Scottish Borders and was first introduced to the wonders of chemistry as a pupil at Berwickshire High School in Duns. He graduated with a BSc in chemistry at the University of St Andrews, where he stayed on to study for a PhD in carbohydrate chemistry with Professor Rob Field. A Wellcome Trust International Prize Travelling Research Fellowship then gave him the opportunity to join the lab of another farmer’s son, Professor Sir Fraser Stoddart FRS, at the University of California, Los Angeles. There, he worked on multivalent glycoconjugates, which became a recurring theme through the next 25 years of his research career.

After five years in synthetic chemistry labs, he realised it was time for a change, and so he used the return leg of his Wellcome Fellowship to branch out into protein biophysics in the lab of Professor Steve Homans in the Astbury Centre for Structural Molecular Biology at the University of Leeds. In 2004, he moved from the University of Leeds campus to the School of Chemistry, where he has been ever since, becoming Professor of Biomolecular Chemistry in 2016. During this time, a Royal Society University Research Fellowship helped him to lay the foundations for his broad research programme in the use of chemical and enzymatic methods to make and modify carbohydrates and proteins for use in targeted delivery and synthetic biology.

Bruce’s work has always been highly collaborative, working closely with colleagues in Leeds and across Europe. He has been the coordinator for several European glycoscience networks, most recently the ‘synBIOcarb’ Marie Sk艂odowska Curie Initial Training Network in synthetic glycobiology.

He was the chair of the RSC Carbohydrate Interest Group in its 50th anniversary year and currently represents the UK at the European Carbohydrate Organisation.

Q&A

How did you first become interested in chemistry?

Maybe it was the chemistry set I had as a kid, but I also had some great chemistry teachers who believed that bangs and smells should be at the centre of the curriculum. They also gave us a remarkable amount of freedom to devise and follow our own sixth year studies research projects – that was an early taste of the satisfaction of scientific research. I’ve also always loved chemistry glassware – especially anything that can do continuous extractions like a soxhlet – they can be quite mesmerising.

What motivates you?

Working with enthusiastic, intelligent young people is a constant source of motivation for me. Helping them to succeed in their research projects is always rewarding.

Why do you think collaboration and teamwork are important in science?

We know enough about chemistry itself that the most exciting discoveries and developments are going to come at the interface with other subjects. None of us can be an expert in everything and so learning to communicate and work together with people with complementary skills is essential for scientific progress. People with different backgrounds bring very different perspectives to a project and can often see solutions to problems that you would never think of yourself. It is also a great way to keep developing your own knowledge and broadening your own horizons. One of my current scientifically diverse collaborations involves developing methods to target microbubbles to bacterial infections – that involves researchers from chemistry, physics, engineering, microbiology and medicine. In another collaboration with a team of geographers, we are trying to unlock the information on historical rainfall records that is embedded in the cellulose of tree rings. You just can’t do science like this on your own – and it is always more fun working with other people!

What is your favourite element?

In the earlier part of my career, it was definitely sulfur: thioglycosides in my PhD, helping to discover methylthioxylose to be a mycobacterial sugar as a postdoc, oxathiane glycosyl donors early in my independent career. I love the fact the oxidation levels of sulfur are named alphabetically: sulfuryl, sulfonyl, sulfinyl, sulfenyl, sulfanyl. A bit later, nitrogen became my new favourite with reductive aminations, oxime ligations and azide cycloadditions – who wouldn’t love the element with an odd valency and even mass. But in recent years, fluorine has caught my eye....

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