Research Fellows Directory
Professor David Spring
University of Cambridge
Drugs today target deep pockets in proteins, i.e. active sites of enzymes, GPCRs and ion channels. However, there are so many more potential protein targets. A particularly outstanding target is the interface that proteins use to contact other proteins in a so-called protein-protein interaction (PPI). Multi-protein complexes regulate all essential cellular functions. The function, activity and specificity of these complexes are mainly controlled by the PPIs that occur between subunits. Human diseases can be caused by anomalous PPIs, e.g. loss/formation/stabilization of a protein complex at the wrong time or location. Significantly, PPIs impart selectivity of cellular function. Selective intervention in cellular processes is fundamental both to the design of chemical tools for dissecting mechanisms, and the development of new therapeutic chemical entities. Therefore, the development of a general approach to modulate PPIs with small molecules would represent a major advance in chemistry, biology and medicine.
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