Novel oligoamide foldamers for the disruption of selected protein-protein interactions

ORGN 432

Fred Campbell, chm1fc@leeds.ac.uk1, Barbora Malkova2, Thomas A. Edwards2, and Andrew J. Wilson, A.J.Wilson@leeds.ac.uk1. (1) Department of Chemistry, University of Leeds, Woodhouse Lane, Leeds, United Kingdom, (2) Astbury Centre for Structural Molecular Biology, University of Leeds, Woodhouse Lane, Leeds, United Kingdom
Protein-protein interactions play a central role in cellular processes and as such represent an attractive target for therapeutic intervention. This presentation will discuss the synthesis and binding properties of a series of N-alkylated para-benzamide foldamers designed to act as proteomimetics of the p53 helix which natively binds the HDM2 protein. This protein-protein interaction is a prime chemotherapeutic target and our results represent a key step in establishing general approaches for the inhibition of these complexation events.
 

Heterocycles and Aromatics, Molecular Recognition and Self Assembly
8:00 PM-10:00 PM, Tuesday, April 8, 2008 Morial Convention Center -- Hall A, Poster

Division of Organic Chemistry

The 235th ACS National Meeting, New Orleans, LA, April 6-10, 2008