Letters in Drug Design & Discovery

G. Perry
University of Texas
San Antonio, TX
Email: lddd@benthamscience.org


Inhibitors of Hepatitis C Virus NS3.4A Protease: P2 Proline Variants

Author(s): Luc J. Farmer, Shawn D. Britt, Kevin M. Cottrell, John J. Court, Lawrence F. Courtney, David D. Deininger, Cynthia A. Gates, Scott L. Harbeson, Kai Lin, Chao Lin, Yu- P. Luong, John P. Maxwell, Janos Pitlik, B. G. Rao, Wayne C. Schairer, John A. Thomson, Roger D. Tung, John H. Van Drie, Yunyi Wei, Robert B. Perni.


A series of novel bicyclic proline P2 scaffold based tetrapeptide inhibitors were designed and prepared. Given their relatively small size, these compounds exhibited exceptional binding affinities and good cellular potencies for HCV protease. One of the best analogues, tricyclic based P2 scaffold 12, had an affinity for HCV with a Ki of 37 nM and cell activity IC50 of 200 nM.

Keywords: Hepatitis C, NS3, •, 4A protease, tetrapeptide inhibitors, VX-950, bicyclic proline, P2 scaffolds

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Article Details

Year: 2005
Page: [497 - 502]
Pages: 6
DOI: 10.2174/157018005774479203
Price: $58