Dr Peter Cossar

Proteins, the building blocks of cells, exist on a spectrum from highly folded to completely unfolded. The latter, known as intrinsically disordered proteins (IDPs), have a spaghetti-like structure and play critical roles in cellular processes such as signaling and protein localization. However, when these proteins malfunction, they can drive diseases such as neurodegeneration, cancer, and metabolic disorders. Unlike well-structured proteins that possess cavities, known as binding pockets, for small molecule drug engagement, IDPs lack such pockets. This limitation hinders therapeutic intervention and has led to many IDPs being classified as "undruggable."

The Cossar lab aims to overcome this challenge using a novel drug discovery paradigm called induced proximity. Unlike traditional drug discovery, which focuses on inhibiting protein function, this orthogonal approach uses small molecules known as molecular glues to bring proteins together. This strategy can enhance or create new cellular functions.

Our projects combine innovative chemistry with molecular biophysics, and chemical biology, to identify new chemical probes for investigating IDP-centered protein-protein interactions. With the ultimate goal to validate or de-risk therapeutic new therapeutic concepts. The lab is interdisciplinary, integrating expertise in protein-protein interaction chemical biology, fragment- and covalent drug discovery, molecular biophysics assay development, and small molecule mechanistic studies.