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

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

Volume: 2 Issue: 2

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

Affiliation:

Keywords: hcv, ns3/ns4a protease, dipeptide inhibitors

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.

Cite this article as:

Colarusso Stefania, Gerlach Benjamin, Giuliano Claudio, Koch Uwe, Matassa G. Victor and Narjes Frank, The Role of an Amphiphilic Capping Group in Covalent and Non-Covalent Dipeptide Inhibitors of HCV NS3 Serine Protease, Letters in Drug Design & Discovery 2005; 2 (2) . https://dx.doi.org/10.2174/1570180053175089