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

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

Journal Name: Letters in Drug Design & Discovery

Volume 2 , Issue 2 , 2005

Become EABM
Become Reviewer


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

Rights & PermissionsPrintExport Cite as

Article Details

Year: 2005
Page: [113 - 117]
Pages: 5
DOI: 10.2174/1570180053175089
Price: $65

Article Metrics

PDF: 2