Protein-protein interactions (PPIs) regulate all signalling pathways for cellular function. Developing molecules that modulate PPIs through the interface of their protein surfaces has been a significant challenge and there has been little success controlling PPI’s through standard molecular library screening approaches. PPIs control the cell’s protein-folding machinery, and this machinery relies on the formation of a multiprotein complex that includes heat shock protein 27 (Hsp27), and Hsp70. Described is the <i>de-novo</i>design, synthesis and biological evaluation of molecules aimed to regulate the function of Hsp27 and Hsp70. We report how to design molecules that directly regulate these proteins interacting with the folding machinery and inhibit protein folding events.

Controlling protein folding via <i>de novo </i>design of small molecules

2019 Spring National Meeting

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.

Controlling protein folding via de novo design of small molecules