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

Stefania Colarusso; Benjamin Gerlach; Claudio Giuliano; Uwe Koch; Victor G. Matassa; Frank Narjes

doi:10.2174/1570180053175089

ISSN: 1570-1808
E-ISSN: 1875-628X

The Role of an Amphiphilic Capping Group in Covalent and Non-Covalent Dipeptide Inhibitors of HCV NS3 Serine Protease
Authors: Stefania Colarusso¹, Benjamin Gerlach², Claudio Giuliano³, Uwe Koch⁴, Victor G. Matassa⁵ and Frank Narjes⁶
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¹ Department of Chemistry, IRBM- MRL Rome, Via Pontina km. 30.600, Pomezia, 00040 Rome, Italy. ² Department of Chemistry, IRBM- MRL Rome, Via Pontina km. 30.600, Pomezia, 00040 Rome, Italy. ³ Department of Chemistry, IRBM- MRL Rome, Via Pontina km. 30.600, Pomezia, 00040 Rome, Italy. ⁴ Department of Chemistry, IRBM- MRL Rome, Via Pontina km. 30.600, Pomezia, 00040 Rome, Italy. ⁵ Department of Chemistry, IRBM- MRL Rome, Via Pontina km. 30.600, Pomezia, 00040 Rome, Italy. ⁶ Department of Chemistry, IRBM- MRL Rome, Via Pontina km. 30.600, Pomezia, 00040 Rome, Italy.
Source: Letters in Drug Design & Discovery, Volume 2, Issue 2, Mar 2005, p. 113 - 117
DOI: https://doi.org/10.2174/1570180053175089
- Available online: 01 Mar 2005

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.

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2005-03-01

2025-05-20

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Article Type: Review Article

Keyword(s): dipeptide inhibitors; hcv; ns3/ns4a protease

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

Abstract

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