Dr Hannah Britt

Profile

I am a lecturer in the School of Chemistry and a member of the Astbury Centre for Structural Molecular Biology, with scientific interests which fall at the interface between the fields of chemistry and biology. During my first foray into research at the University of Durham this intrest led me to the application of biophysical methods, especially mass spectrometry, to study the reactivity of pharmaceuticals and antimicrobial peptides at the cell membrane, under the supervision of Drs John Sanderson and Jackie Mosely. After completing my PhD, I moved on to postdoctoral research with Professor Kostas Thalassinos (UCL) and Professor Dame Carol Robinson (Oxford). In these roles I further developed my mass spectrometry expertise to explore protein behaviour at the cell membrane, with a particular focus on probing features of disease-related and glycosylated proteins within their native environments. Since joining the University of Leeds as lecturer in 2024, my research focuses on the development of mass spectrometry approaches to capture dynamic disease mechanisms directly from human tissues and biofluids, in an effort to revolutionise disease diagnosis and treatment.

Research interests

Understanding the intricate and interwoven landscape of dynamic biological molecules which form the molecular basis of life is a fascinating but challenging puzzle. Unpicking this world in miniature holds the key to tackling some of the greatest challenges of our time, from ensuring food sustainability to improving human health. One innovative approach to understanding this fundamental biology is to study the molecular mechanisms of life using chemical approaches. Mass spectrometry (MS) is a powerful analytical technique capable of achieving this goal. When applied to biological systems, MS can unravel protein-effector interactions, protein dynamics, and post-translational modifications, building up a comprehensive molecular picture of biological pathways. Like many existing techniques, however, MS is currently limited in its ability to capture the full complexity of biological systems on physiologically relevant millisecond timescales.

Imagine if it were possible not only to watch molecular mechanisms play out in real time in their native environment, but to simultaneously unpick the therapeutic strategies which modulate them.

My group develop and apply structural MS approaches, particularly native and top-down MS, to achieve this vision. By studying dynamic molecular mechanisms in this way, we aim to revolutionise disease diagnosis and treatment. Our focus is on unpicking biochemical pathways directly from human tissues and biofluids, maintaining the complexity of their native environment into the mass spectrometer. We are also interested in how these molecular pathways are altered and modulated, particularly in disease states or by pharmaceuticals.

Qualifications

• PhD, University of Durham
• MSci, University of Durham

Professional memberships

• Biochemical Society
• British Mass Spectrometry Society

Student education

I teach mass spectrometry, medicinal chemistry, and biological chemistry at undergraduate level. I act as an academic tutor, and offer research projects for MChem and MNatSci final year students.

Research groups and institutes

• Chemical Biology and Medicinal Chemistry
• Organic