Advances in the asymmetric synthesis of silanediol protease inhibitors

ORGN 116

Yingmei Qi, qiymei@temple.edu, Wondwossen D. Arasho, wdegefa@hotmail.com, and Scott McN. Sieburth, scott.sieburth@temple.edu. Department of Chemistry, Temple University, 1901 N. 13th Street, Philadelphia, PA 19122
Crucial to the design of a protease inhibitor is the selection of a nonhydrolysable analog of the tetrahedral hydrated carbonyl intermediate. We have prepared and evaluated silanediol peptide mimics, which yield low nanomolar inhibitors of metallo- and aspartic proteases. Advances in efficient synthesis of the nonhydrolysable silanediols have been made with full control of stereochemistry. Progress in the further application of these inhibitors to serine protease such as chymotrypsin will be presented.

 

Total Synthesis, Materials, Devices and Switches, Molecular Recognition and Self-Assembly, Biologically-Related Molecules and Processes
8:00 PM-10:00 PM, Sunday, August 19, 2007 BCEC -- Exhibit Hall - B2, Poster

Division of Organic Chemistry

The 234th ACS National Meeting, Boston, MA, August 19-23, 2007