Professor Edward Tate

Biography

Professor Edward Tate FRSC is the GSK Chair in Chemical Biology at Imperial College London and a Satellite Group Leader at the Francis Crick Institute. He studied chemistry at Durham University before completing a PhD in organic chemistry at the University of Cambridge, followed by postdoctoral fellowships at the École Polytechnique and Institut Pasteur in Paris. He established his independent group at Imperial in 2006 as a BBSRC David Phillips Fellow and became professor of chemical biology in 2014. He has been a Fellow of the Royal Society of Chemistry since 2013.
 
His research sits at the interface of chemistry, biology and medicine, using synthetic chemistry, chemical proteomics and molecular cell biology to understand how proteins are modified in cells, and how these processes can be exploited for drug discovery. He is internationally recognised for pioneering chemical technologies to study protein lipidation, a major class of post-translational modification that controls how proteins interact with membranes and cellular signalling networks. His laboratory developed widely used chemical probes for myristoylation, prenylation and S-acylation, enabling these modifications to be studied across the proteome in living cells.
 
Professor Tate’s work has helped establish protein lipidation as a new frontier for therapeutic discovery, including in cancer, infection, autophagy and cellular senescence. His research led directly to the founding of Myricx Bio, which is developing first-in-class antibody-drug conjugate (ADC) therapeutics targeting protein lipidation, and Siftr Bio, which is developing next-generation protease-responsive technologies for targeted therapeutics.
 
He has received several major honours, including the RSC Corday-Morgan Prize, the RSC Chemistry Biology Interface Horizon Prize, the RSC Norman Heatley Award, the Sir David Cooksey Translation Prize, and the Cancer Research Horizons Startup Achievement Prize.

If a problem is important and the right tools do not exist, building those tools can make a powerful scientific contribution.

Edward Tate

Q&A

Can you tell us more about your work?

Much of my work is concerned with understanding how the chemistry of proteins controls the behaviour of cells. Proteins are often described as the molecular machines of life, but their activity is not determined by their sequence alone. After they are made, proteins can receive chemical ‘upgrades’, known as post-translational modifications, that allow them to take on new roles. These modifications can act like specialised attachments or access passes: they can send a protein to a new location in the cell, allow it to interact with new partners, or switch its activity on or off.
 
My laboratory has focused particularly on protein lipidation, a process in which small fat-like chemical groups are attached to proteins. In simple terms, lipidation gives proteins a membrane-targeting upgrade. It helps them move to the right cellular membrane at the right time, where they can organise signalling pathways and control key cellular decisions. For many years, this process was difficult to study because the necessary chemical tools did not exist. We developed probes and proteomic technologies that allow lipidated proteins to be detected, identified and quantified across thousands of proteins in living cells. These tools have helped transform protein lipidation from a relatively specialised area into a broadly accessible field of biology and drug discovery.
 
The wider implications are significant because many diseases depend on abnormal protein signalling, trafficking and cell survival pathways. Our work has shown that lipidation is important in cancer, viral infection, malaria, autophagy, ferroptosis and cellular senescence. It has also shown that enzymes controlling lipidation can be targeted with drugs. This has opened new therapeutic possibilities, including host-directed antiviral strategies, new approaches to MYC-driven cancers, and antibody-drug conjugates carrying lipidation-targeting payloads.
 
More recently, we have extended this philosophy to molecular glues and other proximity-based approaches. These are small molecules that work not simply by blocking a protein, but by bringing proteins together in new combinations, effectively rewiring cellular machinery to change the fate or function of disease-relevant proteins. Our emerging work in this area aims to make molecular glue discovery more systematic, using proteomics to detect new drug-induced protein interactions across the cell.
 
A central theme of our research is that fundamental chemical biology can create practical routes to new medicines. Discoveries from my laboratory have led to chemical probes used widely across academia and industry, several patent filings, and the creation of biotechnology companies including Myricx Bio and Siftr Bio. These companies are translating chemical biology discoveries into new therapeutic platforms, with Myricx advancing first-in-class lipidation-targeting payloads towards clinical evaluation.

Who or what first sparked your interest in chemistry, and how has that interest evolved over time? 

I was drawn to chemistry because it offered a way to understand and change the material world at the molecular level. I liked the combination of logic and creativity: the idea that you could design a molecule, make it, test it, and learn something new from the result.

Over time, that interest has evolved from making molecules for their own sake to using chemistry as a way to understand biology. What continues to excite me is that chemistry can give us tools that biology alone cannot provide. A well-designed molecule can reveal how a protein works, expose a hidden vulnerability in a disease process, or open a completely new route to a medicine. That ability to change the world by moving from molecular design to biological insight, and sometimes to therapeutic opportunity, is what has kept chemistry so compelling for me.

What has been the most rewarding or memorable highlight of your career so far? 

There have been many memorable moments, but the most rewarding are those where fundamental chemical biology has unexpectedly opened a route towards real-world impact. One example is seeing our long-standing work on protein lipidation, which began with basic questions about how to detect and understand lipid-modified proteins, develop into new therapeutic ideas and ultimately contribute to the founding of Myricx Bio.

That trajectory has taken us from chemical probes and proteomics, through target validation and inhibitor discovery, to a company advancing first-in-class therapeutic programmes. It is also rewarding because it reflects the work of many people in the group over many years. Seeing students, postdocs and collaborators contribute to something that has grown well beyond the original academic question is one of the great privileges of my career.

What have been the biggest challenges that you have faced over the course of your time in science, and what have you learned from those experiences? 

One of the biggest challenges has been working in areas where the field did not yet have the tools needed to answer the most important questions. Protein lipidation is a good example. For a long time, it was clear that these modifications mattered, but it was very difficult to study them systematically. That meant we often had to build the tools before we could address the biology.

I have learned that this requires patience and persistence. Tool building can be slow, technically demanding and sometimes difficult to fund or publish until the impact becomes clear. But when the tools are right, and particularly when they are integrated with multiple orthogonal approaches, they can enable labs around the world to change what is possible. I have also learned the importance of building teams with complementary expertise, because the most interesting problems never sit in a single discipline.

Thinking back to earlier in your career, are there any words of wisdom that you wish someone had told you? 

I would probably advise myself not to worry too much if the most interesting questions do not fit neatly into an established field. Some of the best opportunities come from working at the edges between disciplines, where the language, standards and expectations are not always aligned.

I would also say that it is worth investing in difficult, enabling technologies, even when the path to impact is not immediately obvious. If a problem is important and the right tools do not exist, building those tools can make a powerful scientific contribution. Finally, I would remind myself that science is a long road, with many unexpected twists. Individual papers and grants are just steps on the path, the deeper satisfaction comes from building a body of work, a group culture, and a network of people who can help your science make a positive impact in the world.

What impact would you say that your work is having on your field and/or the wider world? 

I hope our work has helped to make previously inaccessible biology experimentally and therapeutically tractable. In protein lipidation, we developed chemical probes, inhibitors, and proteomic methods that allowed these modifications to be studied globally in living cells. That helped shift the field from studying a small number of individual proteins to understanding lipidation as a broader regulatory system in cell biology and disease.

The wider impact is that these tools and concepts have opened new opportunities in drug discovery. Our work has helped validate lipidation enzymes as therapeutic targets in infection and cancer, and has contributed to new approaches including host-directed antivirals, cancer vulnerabilities linked to N-myristoylation, and lipidation-targeting payloads for antibody-drug conjugates. More broadly, our work in chemical proteomics, activity-based profiling and molecular glues aims to show how chemistry can reveal both new biology, and new ways to intervene in disease.

What future directions or opportunities do you see for your work? 

A major opportunity is to move from mapping protein modifications to understanding and controlling them with much greater precision. For lipidation, that means identifying which enzymes modify which substrates, how those events are regulated in different disease contexts, and how we can selectively modulate them for therapeutic benefit.

I am also excited by the potential of molecular glues and other induced-proximity approaches. These molecules do not simply block proteins; they rewire interactions between proteins and can create new biological outcomes. The challenge is to make their discovery more systematic. Our emerging work uses proteomics to detect drug-induced protein interactions across the cell, with the aim of turning molecular glue discovery from something partly serendipitous into a more predictable and scalable process.

More broadly, I see chemical proteomics becoming an increasingly powerful discovery engine, especially when combined with structural biology, functional genomics and machine learning.

What do you wish more people understood about your field or the chemical sciences in general? 

It would be good if more people appreciated that chemistry is not only about making compounds or materials, important though those are. Chemistry is also a way of asking precise questions about living systems. A good chemical probe can test what a protein does, when it does it, where it acts, and whether it can be targeted therapeutically.

In chemical biology, the molecule is often the key enabler of both the experiment and the hypothesis. If it is designed well, it can reveal biology that would otherwise remain hidden. This is why chemistry is so important for medicine: it helps move us from correlation to mechanism, and from mechanism to intervention.

As bioscience becomes increasingly genomics-centred, molecular understanding is at risk of being undervalued. Chemists bring the ability to understand, design and perturb biology at the molecular level, and that is becoming an increasingly rare and valuable perspective.

In what ways does creativity influence how you think about or carry out your work? 

Creativity is essential in chemical biology because the best questions often cannot be answered with the methods already available. You have to imagine the experiment that would make the problem solvable, and then work out what molecule, assay or platform is needed to do it.

Creativity is not separate from rigour. It is about finding a new angle on a difficult problem, but then testing it precisely. Some of our most productive work has come from connecting areas that were not previously strongly linked: lipidation and cancer vulnerabilities, protease activity and targeted therapeutics, or proteomics and molecular glue discovery. The creative step is often recognising that two fields, technologies or concepts can be brought together to make something possible that neither could achieve alone.

Are there any scientific developments, either recent or on the horizon, that you are excited about? 

I am particularly excited by the convergence of chemical biology, high-throughput experimental approaches and AI/ML. We can now generate proteome-wide and genome-wide datasets at a scale that was not realistic earlier in my career. The challenge, and the opportunity, is to turn those datasets into mechanistic understanding and useful therapeutic hypotheses.

Molecular glues are a good example. These molecules can induce new protein interactions and potentially modulate targets that have been considered undruggable, but their discovery has often been serendipitous. By combining proteome-wide interaction screening, functional genomics, structural biology and machine learning, there is a real opportunity to make this area systematic, and thereby unlock almost unlimited therapeutic opportunities. More broadly, I think the interface between chemical perturbation, large-scale cellular measurement and predictive modelling will be one of the most important directions for drug discovery over the next decade.

What does good research culture mean to you, and why does it matter? 

Good research culture means creating an environment where people can do ambitious science while being supported, respected and properly credited. It requires high standards, but also openness, trust and a commitment to helping people develop.

This matters because people pass through a research group. The group head remains, but students, postdocs, technicians and research staff are with us for a defined period. Part of my job is to make sure they leave better prepared for whatever comes next, whether that is academia, industry, a role outside research, or something quite different. Good culture means taking those ambitions seriously, even when they do not align perfectly with the immediate goals of a project.

It also matters because research is difficult. A good group culture gives people the confidence to discuss problems early, share expertise, challenge assumptions and help each other through setbacks. In a multidisciplinary group, that peer support is essential. It helps people build the confidence, judgement and skills they need for the next stage of their careers.

How can scientists try to improve the environmental sustainability of research? Can you give us any examples from your own experience or context? 

Research has a real environmental footprint, particularly in chemistry and biomedical science, where we rely on solvents, plastics, energy-intensive equipment and cold storage. Sustainability should therefore be part of good laboratory practice.

In my own context, the biggest gains come from better experimental design, shared infrastructure and more efficient use of resources. Well-run shared facilities reduce duplication of expensive instruments, improve utilisation and support higher quality data. Careful experimental planning also matters: fewer poorly designed experiments means less waste, less repetition and better science.

New technologies can also help. For example, acoustic dispensing can greatly reduce the use of disposable plastic tips, while automation and miniaturisation can massively lower reagent consumption and improve reproducibility. These changes are practical, achievable and aligned with doing better science.

How important would you say collaboration is for producing high quality science? How has collaboration influenced your work? 

Collaboration has been central to almost everything important my group has done. The questions we work on sit between chemistry, biology, proteomics, structural biology, medicine and drug discovery, and no single laboratory can cover all of that at the highest level.

This was especially important early in my independent career, when collaborations with experienced bioscientists were a critical form of mentorship. I was fortunate to work with colleagues who were extremely generous with their time, expertise and scientific vision, including Roberto Solari, Tony Magee, Tony Holder, Robin Leatherbarrow, Debbie Smith, Miguel Seabra, Rita Tewari and Andy Bell. They helped us ask better biological questions, interpret our results more critically, and connect chemical tools to real biological and therapeutic problems.

Good collaborations have shaped both the questions we ask and the way we answer them. Our work on protein lipidation has depended on combining chemistry with mass spectrometry, cell biology, structural biology and disease models. Our translational work has also depended on close interaction with clinicians, industrial scientists and investors. In each case, the science has been stronger because the expertise was genuinely shared.

If you had unlimited resources, what research question would you most want to explore? 

I would want to build towards a generative foundation model of the cell: a model that can predict how chemical, genetic or environmental perturbations change protein function, signalling, cell state and ultimately phenotype. The ambition would not just be to describe the cell, but to generate experimentally testable predictions about how to control it.

The next step would be to extend this from single cells to tissues, organs and eventually ecosystems, where different cell types, immune responses, metabolism and microenvironment all interact. From a translational perspective, that would be extremely powerful. It could help identify which biological mechanisms are causal in disease, which interventions are most likely to work, and how to design combinations or targeted therapies with much greater confidence.

To get there, we would need to integrate chemical biology, proteomics, functional genomics, imaging, structural biology, clinical samples and AI/ML at a scale that is not yet achievable. It is a long-term goal, but one that would fundamentally change how we connect molecular mechanism to therapeutic intervention.

What is your favourite element and why? 

Carbon. It is the obvious answer for an organic chemist, but it is the right one. Carbon gives us stable bonds, three-dimensional structures, functional group diversity, and the ability to build molecules with very precise shapes and properties.

It is also the element that connects the chemistry I was trained in with the biology I now work on. Carbon-based molecules are the basis of life, but they are also the tools we use to study and influence life. That versatility is what makes chemical biology possible: we can design and make molecules that nature has never seen, but that can still interact with biological systems in highly specific and informative ways.