Interactions between members of the Bcl-2 family of proteins control the life/death fate of cells by regulating apoptosis. Cancer cells can evade apoptosis through over-expression of pro-survival members of the Bcl-2 family, such as the proteins Bcl‑xL and Mcl‑1. This is not only an important step in the progression to cancer but also a mechanism through which cancer cells can become resistant to standard anti-cancer therapies 123.
Small molecules able to mimic the activity of pro-apoptotic BH3-only proteins hold potential for reactivating apoptosis in tumours; either as single agents in certain tumours, or to sensitise cancers to existing therapies 4 . Previous work at WEHI has led to the development of small molecules possessing a benzoylurea core which are able to mimic alpha-helical BH3 peptides and which bind to Bcl-xL with low micromolar binding affinity 5 . Co-crystal structures for a number of these compounds in complex with Bcl-xL have been obtained and have formed the basis for further structure-based optimization.
This poster will outline new developments in our lab using structure-based approaches to target pro-survival members of the Bcl-2 family.