Abstract
New treatments for HCV (Hepatitis C virus) infections are likely to arise from inhibition of the essential, virally-encoded enzymes. These targets include the serine protease required for processing of the HCV polyprotein. The protease constitutes one functional domain of the bifunctional HCV NS3 (non-structural protein 3). Here, insights regarding the NS3 structure and recently synthesized NS3 inhibitors are reviewed. Interestingly, many NS3 protease inhibitors have taken advantage of an unusual product inhibition by Nterminal products of cleavage at the polyprotein processing sites.
Keywords: Peptidic Inhibitors, Hepatitis C, Serine Protease, Protein, Norvaline, Cyclohexylalanine, carboxy glutamic acid
Current Pharmaceutical Design
Title: Peptidic Inhibitors of the Hepatitis C Virus Serine Protease within Non- Structural Protein 3
Volume: 8 Issue: 28
Author(s): T. O. Fischmann and P. C. Weber
Affiliation:
Keywords: Peptidic Inhibitors, Hepatitis C, Serine Protease, Protein, Norvaline, Cyclohexylalanine, carboxy glutamic acid
Abstract: New treatments for HCV (Hepatitis C virus) infections are likely to arise from inhibition of the essential, virally-encoded enzymes. These targets include the serine protease required for processing of the HCV polyprotein. The protease constitutes one functional domain of the bifunctional HCV NS3 (non-structural protein 3). Here, insights regarding the NS3 structure and recently synthesized NS3 inhibitors are reviewed. Interestingly, many NS3 protease inhibitors have taken advantage of an unusual product inhibition by Nterminal products of cleavage at the polyprotein processing sites.
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Cite this article as:
Fischmann O. T. and Weber C. P., Peptidic Inhibitors of the Hepatitis C Virus Serine Protease within Non- Structural Protein 3, Current Pharmaceutical Design 2002; 8 (28) . https://dx.doi.org/10.2174/1381612023392595
DOI https://dx.doi.org/10.2174/1381612023392595 |
Print ISSN 1381-6128 |
Publisher Name Bentham Science Publisher |
Online ISSN 1873-4286 |
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