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Letters in Drug Design & Discovery

Author(s): Stefania Colarusso, Benjamin Gerlach, Claudio Giuliano, Uwe Koch, Victor G. Matassa and Frank Narjes

DOI: 10.2174/1570180053175089

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The Role of an Amphiphilic Capping Group in Covalent and Non-Covalent Dipeptide Inhibitors of HCV NS3 Serine Protease

Page: [113 - 117] Pages: 5

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Abstract

The analysis of the S3 binding region of the Hepatitis C Virus NS3 serine protease allowed replacing the P3 amino acid of a-ketoacid tripeptide inhibitors with an amphiphilic capping group. The binding mode of α-ketoacid (8) (IC50 = 1 μM) and the role of the amphiphilic group in non-covalent phenethylamide inhibitor (15) (IC50 = 21 μM) will be discussed.

Keywords: hcv, ns3/ns4a protease, dipeptide inhibitors