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My research focuses on the application of molecular biophysical and protein engineering techniques to the study of the structure and function of immunoglobulin E (IgE) and its receptors, with the principal aim of understanding the molecular mechanisms sufficiently well to develop new anti-allergy therapeutics.  We recently began to appreciate in detail how conformational changes are critical to obtaining the high-affinity interaction between IgE and its mast cell receptor, which is the key to triggering allergic responses to allergens.  Much of my laboratory’s efforts are currently spent helping an industrial partner to develop allosteric inhibitors of IgE, entirely underpinned by our knowledge of the conformational changes that IgE can undergo. 

We have developed some very popular antibody expression vectors (available from to aid in the rapid evaluation of the safety and efficacy of recombinant antibodies.  This supports an antibody discovery programme, aimed at testing the potential of using IgE isotype anti-tumour antibodies to achieve more effective cell killing of solid tumours (a Phase I clinical trial is currently taking place), in essence, by making patients allergic to their tumours.   Our most recent work focuses on creating novel proteins that can catalyse the destruction of IgE antibodies.  We are also beginning to investigate the structure and interactions of soluble IgD antibodies, which recent studies suggest may also be involved in allergic disease. My laboratory hosts a protein engineering core facility, which is available to members of staff and students.

I am an undergraduate admissions tutor for the Biochemistry BSc and MSci programmes and teach protein related theoretical and experimental topics at undergraduate and postgraduate level.