Targeting protein-protein interactions with hydrogen bond surrogate artificial alpha-helices

ORGN 777

Laura K. Henchey, laura.henchey@nyu.edu, Deyun Wang, dw522@nyu.edu, and Paramjit S. Arora, arora@nyu.edu. Department of Chemistry, New York University, 100 Washington Square East, New York, NY 10003
The alpha helix is the most prominent protein secondary structure. We have recently described a new approach for the stabilization of artificial alpha-helices that involves replacement of one of the main chain hydrogen bonds with a carbon-carbon bond derived from a ring-closing metathesis reaction. The Hydrogen Bond Surrogate (HBS) method affords stable alpha helices and does not diminish its molecular recognition surface. These artificial alpha helices are being used to target two important apoptotic proteins, BAK BH3 binding domain of BcL-xL and the p53 binding domain of MDM2. This poster will discuss the molecular recognition properties of our HBS alpha- helices for both of these receptors.

 

Total Synthesis, Materials, Molecular Recognition, Process R&D, and Physical Organic Chemistry
8:00 PM-10:00 PM, Wednesday, 13 September 2006 Moscone Center -- Hall D, Poster

Sci-Mix
8:00 PM-10:00 PM, Monday, 11 September 2006 Moscone Center -- Hall D, Sci-Mix

Division of Organic Chemistry

The 232nd ACS National Meeting, San Francisco, CA, September 10-14, 2006