Bioorganic Chemistry: Design of inhibitors for protein-protein interactions
Proteins often utilize small folded domains for recognition of other proteins, DNA and RNA. The hypothesis guiding our research is that by mimicking these folded domains we can modulate the function of a particular protein with metabolically stable synthetic molecules. The manifestation of this hypothesis into specific and potent compounds that interfere with chosen targets in cellular and animal systems requires new computational and synthetic approaches. We seek to devise a systematic framework to evaluate and target protein-protein interactions with structured peptidic and nonpeptidic scaffolds designed to reproduce the critical interfacial features of proteins.