ORGN 259 |
| Transient interactions between protein surfaces guide virtually every cell signaling event, and the discovery of molecules that inhibit protein-protein interactions is a foremost goal of chemical biology. This goal is complicated by the reality that protein-protein interaction domains are large, shallow, and (especially for transient complexes) closely resemble non-interacting regions of the protein exterior. This lecture will describe our work using miniature proteins and ß-peptide foldamers to recognize protein surfaces with high affinity and specificity and inhibit the formation of protein-protein interactions in vitro and in vivo. We will focus in particular on molecules that possess paralog specificity – the ability to discriminate their prescribed target from structurally related family members. |
|
Frontiers in Bio-organic Chemistry and Chemical Biology
8:00 AM-11:55 AM, Monday, 14 March 2005 Convention Center -- Ballroom 20 C-D, Oral
Division of Organic Chemistry |