Abstract
HCV NS3/4A serine protease is essential for the replication of the HCV virus and has been a clinically validated target. A series of HCV NS3/4A protease inhibitors containing a novel acylsulfamoyl benzoxaborole moiety at the P1' region was synthesized and evaluated. The resulting P1-P3 and P2-P4 macrocyclic inhibitors exhibited sub-nanomolar potency in the enzymatic assay and low nanomolar activity in the cell-based replicon assay. The in vivo PK evaluations of selected compounds are also described.
Copyright © 2010 Elsevier Ltd. All rights reserved.
MeSH terms
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Animals
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Boron Compounds / chemical synthesis
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Boron Compounds / chemistry*
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Boron Compounds / pharmacokinetics
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Catalytic Domain
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Hepacivirus / drug effects
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Hepacivirus / enzymology*
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Male
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Models, Molecular
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Protease Inhibitors / chemical synthesis*
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Protease Inhibitors / chemistry
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Protease Inhibitors / pharmacokinetics
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Rats
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Rats, Sprague-Dawley
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Viral Nonstructural Proteins / antagonists & inhibitors*
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Viral Nonstructural Proteins / metabolism*
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Virus Replication / drug effects
Substances
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Boron Compounds
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NS3 protein, hepatitis C virus
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Protease Inhibitors
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Viral Nonstructural Proteins