Protein-Protein Interactions as Drug Targets 2014

Most small molecule drugs achieve their effect by inhibiting the action of disease-causing/errant proteins at their catalytic sites if they are enzymes (such as proteases and kinases) or by interfering with extracellular binding sites if they are receptors or ion channels. But over the past ten years or more it has become clear that many proteins are also worth targeting for their role in regulatory complexes of important biological processes that effect disease states such as intracellular signal transduction, transcription, immunomodulation, epigenetic modifications or protein stability.

Targeting protein-protein interactions (PPIs) with small molecules has been aided by advances in technologies that allow for studying protein binding interactions such as surface plasma resonance (SPR) and nuclear magenetic resonance (NMR) in a screening format. However many challenges remain – optimizing small molecule candidates that disrupt or enhance PPIs pose a different set of challenges because the targets’ structure is usually not known and is usually a larger area with different physico-chemical properties than a ‘catalytic site’.

Join fellow discovery chemists at Cambridge Healthtech Institute’s Protein-Protein Interactions meeting to learn about the different disease areas where targeting PPIs is showing promise. Hear case studies of PPI screens that have been used and how the compounds that passed through are either progressing or not, with a focus on the kinds of roadblocks they encountered.

Topics will include, but are not limited to:
Using fragments and macrocyclics to target PPIs
Lead optimization challenges for molecules targeting PPIs
PPIs in the anti-infective field
Targeting epigenetic interactions
Industry case studies