Research Interest
Protein/Protein Interactions
It has become clear over the last 20 years that many cellular processes are governed by the physical interaction of two or more proteins.
Multi-protein complexes are involved in many of the key processes in cells and one method to interfere with such processes would be to use small molecules to prevent these complexes forming. The major problem with this idea is that the interaction surface between two proetins is typically very large and some tems of fold larger than the surface area of a small molecule.
Nevertheless, real advances have been made in developing small molecules to inhibit protein/proetin interactions. Our work is focussing on some fundamental research aimed at synthesising mimetics of particular secondary structures found at protein/protein inetrfaces and strongly implicated in their binding.
We are developing novel, druglike compounds that are designed to mimic the alpha-helix motif which is a key interaction between the tumour suppressor p53 and its natural inhibitor MDM2. We are also starting to look at synthetic mimetics of the beta-sheet motif, initially to simply try and understand what exactly drives interactions involving this motif.
Chaperones
Cancer cells are crucially dependent on chaperone protein function as they are a hot-house of protein synthesis and replication.