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Yusuf Hamied Department of Chemistry


As Professor of Chemical and Molecular Biology in the Yusuf Hamied Department of Chemistry, Professor Sophie Jackson's research involves protein folding and peptide aggregation at the interface of chemistry and biological science.

This still sometimes surprises her, as she never envisaged herself as an academic.

At her comprehensive school in Cheshire, Sophie chose to study double maths, physics and chemistry at A level because she thought they might be more ‘useful’ than art subjects. “I thought I didn’t like biology so I didn’t even consider it,” she recalls.  And although she excelled at Maths and Physics, she gradually realised that she loved chemistry best, eventually becoming only the second student from her school to be accepted to an Oxbridge college.

Sophie says she chose The Queen’s College at Oxford, because it had the highest proportion of chemistry students from the north of England. “It was wonderful socially, but I found the subject difficult,” she says. “I felt like I had a huge amount of catching up to do, and didn’t do particularly well in my first-year exams.”

Like many students, Sophie suffered from imposter syndrome, and was constantly comparing herself to her classmates. She says it came as a surprise to be awarded a first-class degree at the end of her studies.  “It was a big shock to me – and to my friends, because I’d convinced them I was going to fail. I realised retrospectively that the chemists in my college were a brilliant cohort who included the top chemist the University had seen for ten years, and I’d been comparing myself to them!”

Sophie discovered biological science during her final-year project, which was on electron transfer in metalloproteins. She was fascinated by both the biological and chemical aspects of the research, and became intrigued by proteins and protein folding. “I learned to love biological science, and realised I wanted to learn more,” she says.

Sophie wanted to go to London, so she applied for a PhD with Professor Alan Fersht at Imperial College, who was at that time noted for his work on enzymology and was just getting into the field of protein folding. Shortly after she started, Professor Fersht informed the whole group they were moving to Cambridge. “So that’s how I ended up in Cambridge!” she laughs. Sophie again had a slow start. “My first two years went horrendously badly,” she recalls ruefully.  Her experiments produced no results and her project was further disrupted by the move to Cambridge. In her third year Sophie felt fortunate to obtain additional funding to pursue a new project she had designed, to develop a simple system for studying protein folding, using a barley protein known as CI2. The project was a success, and her first paper1 on the results became a classic in the field, which has been cited over 800 times

After being awarded her PhD in 1991, Sophie won a research fellowship at Peterhouse, and published numerous papers during her continuing time as a postdoc in the Fersht group. In 1993 she went to Harvard as an International Human Frontiers Postdoctoral Fellow, but this proved to be a fallow two-year period which produced no publications. Sophie is philosophic about this: “These are terrible experiences at the time, but they teach you a lot which stands you in good stead.” In 1995 Sophie returned to Cambridge and Peterhouse, starting her own research group as a Royal Society University Research Fellow.

Once again Sophie had a tough start. The only other female academic in the Department was Melinda Duer, although Jane Clarke (now Master of Wolfson College) joined soon after. “In all my time I had never felt any experience of sexism, then when I came back to run my own research group I got numerous sexist remarks – and most of the men were not even aware what they were saying was sexist.” Despite these obstacles, Sophie’s research began to flourish. She was appointed University Lecturer in 2000 and moved up the ranks to become a Professor in 2017. As one of only four female Professors in the Department, Sophie would still like to see more female role models. “I had no female lecturers as an undergraduate, and when I doubted myself as a young researcher, there were no people like me to emulate. Of course, it has got much better, but there’s still some way to go.”

About five years ago, Sophie became severely affected by Chronic Fatigue Syndrome, and her research group wound down while she took care of her physical health. Now she is much better, although she knows she has to be careful. “I can do a normal working day, but not what I used to do,” she admits. She is thrilled to be re-building her group which currently has five postgraduates.  She is aiming for six to eight members, which she feels would achieve a ‘critical mass’.

Professor Sophie Jackson feels lucky that she has been able to work during much of the coronavirus pandemic from her Derbyshire cottage, in a cosy stone-walled room with an inglenook fireplace. “In fact, I have more work do than ever,” she says, “because we have some really interesting projects that seem to be taking off.”

Fortunately, after the initial lockdown in March 2020, her group members have been able to access the Cambridge lab to continue their experiments. Sophie meets with each of them frequently online to discuss their progress and where to go next.  

“We look at protein folding/unfolding and we also look at peptide aggregation, which is when peptides (chains of amino acids typically shorter than proteins) self-assemble into fibrillar structures and other states,” she explains. “Some of our research is very ‘pure’ in that we’re doing it without an application in mind – for example, we were the first group in the world to study how knotted proteins fold.2 Peptide self-assembly, on the other hand, is much more applied and is particularly relevant in drug formulation and potentially drug delivery.”

When looking at peptides, Sophie explains that sometimes it is desirable to suppress aggregation. This is something the group has been investigating for GLP1 (Glucagon-like peptide), which is used in the treatment of diabetes. At other times peptide self-assembly is advantageous, for example in a drug called Teverelix, which is used in the treatment of prostate cancer. “Teverelix forms a highly unusual colloidal microcrystalline suspension, and there are many advantages to giving it to patients in that form,” explains Sophie, “So we are working on understanding how and why it self-assembles into this microcrystalline state. Ultimately if we understand this, we might be able to induce a similar self-assembly in other peptides for other drug delivery.”

A third research area involves the capping of antibodies. “All therapeutic antibodies have some off-target activity, and that results in side effects and limits the doses at which they can be given,” Sophie explains. “We are trying to develop a new method which involves capping the antibody so that it’s in an inactive state when it’s given to the patient, and only activates when it gets to the target site, which could be a tumour for example.”

One of the things Sophie enjoys most about her work is watching the next generation of scientists develop. “I love watching PhD students develop over the course of three or four years. It’s really rewarding to watch them grow in many different ways, particularly scientifically, and to become confident and extremely competent scientists.” She is also clearly still excited by her research and the new paths it is taking. “I like the fact that we’re constantly learning, we’re learning new things all the time,” she says.  


1Jackson, S.E. & Fersht, A.R. (1991) Biochemistry 30, 10428-10435, Folding of Chymotrypsin Inhibitor 2. 1. Evidence for a two-state transition.

2Jackson, S.E., Suma, A. & Micheletti, C. (2017) How to fold intricately: using theory and experiments to unravel the properties of knotted
Curr. Opin. Struct. Biol. 42, 6-14].