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Protein-protein interactions

We have used fragment-based approaches to target a number of protein-protein interactions. These interactions are considered challenging to target however we have had a success in targeting a number of these.

PBD (Polo-box domain)

We examined the polo-box domain (PBD) of polo-like kinase (Plk1), a valid anti-cancer target whose phosphorylation-dependant protein-protein interactions are crucial are crucial for successful progression of cell mitosis. We examined this PPI using an array of biophysical techniques and identified a novel binding site. This research is was collaboration with Dr Marko Hyvönen and Professor David Spring at the University of Cambridge [Angew. Chem. Int. Ed., 2012] [Angew. Chem. Int. Ed., 2011].

RAD51-BRCA2

We used a fragment-based approach to target the FXXA protein-protein interaction binding site on RAD51. We initially identified a number of fragments which bound to the Phe pocket and from these we were able to develop a number of small molecules inhibitors to disrupt this interaction. This research is was collaboration with Dr Marko Hyvönen. Professor Tom Blundell and Professor Ashok Venkitaraman at the University of Cambridge. This research was funded through a Translation Award and Seeding Drug Discovery Initiative award from the Wellcome Trust [FEBS letters, 2016] [ChemMedChem, 2014].

RAD51-FHTA protein-protein interaction
RAD51-FHTA protein-protein interaction

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