Abstract
A series of peptide boronic acids containing extended, hydrophobic P1 residues was prepared to probe the shallow, hydrophobic S1 region of HCV NS3 protease. The p-trifluoromethylphenethyl P1 substituent was identified as optimal with respect to inhibitor potency for NS3 and selectivity against elastase and chymotrypsin.
MeSH terms
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Antiviral Agents / chemical synthesis*
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Antiviral Agents / pharmacology*
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Boronic Acids / chemical synthesis*
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Boronic Acids / pharmacology*
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Chymotrypsin / antagonists & inhibitors
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Hepacivirus / drug effects
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Hepacivirus / enzymology*
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Humans
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Indicators and Reagents
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Leukocytes / drug effects
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Leukocytes / enzymology
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Pancreas / enzymology
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Pancreatic Elastase / antagonists & inhibitors
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Peptides / chemical synthesis*
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Peptides / pharmacology*
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Protease Inhibitors / chemical synthesis*
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Protease Inhibitors / pharmacology*
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Structure-Activity Relationship
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Viral Nonstructural Proteins / antagonists & inhibitors*
Substances
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Antiviral Agents
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Boronic Acids
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Indicators and Reagents
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NS3 protein, hepatitis C virus
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Peptides
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Protease Inhibitors
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Viral Nonstructural Proteins
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Chymotrypsin
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Pancreatic Elastase