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UK-1 and structural analogs are potent inhibitors of hepatitis C virus replication.

ABSTRACT: The bacterial natural product UK-1 and several structural analogs inhibit replication of the hepatitis C virus in the replicon assay, with IC50 values as low as 0.50 ?M. The NS3 helicase has been identified as a possible target of inhibition for several of these compounds, while the remaining inhibitors act via an undetermined mechanism. Gel shift assays suggest that helicase inhibition is a direct result of inhibitor-enzyme binding as opposed to direct RNA binding, and the ATPase activity of NS3 is not affected. The syntheses and biological results are presented herein.

SUBMITTER: Ward DN 

PROVIDER: S-EPMC6136245 | biostudies-literature | 2014 Jan

REPOSITORIES: biostudies-literature

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UK-1 and structural analogs are potent inhibitors of hepatitis C virus replication.

Ward Dawn N DN   Talley Daniel C DC   Tavag Mrinalini M   Menji Samrawit S   Schaughency Paul P   Baier Andrea A   Smith Paul J PJ  

Bioorganic & medicinal chemistry letters 20131209 2

The bacterial natural product UK-1 and several structural analogs inhibit replication of the hepatitis C virus in the replicon assay, with IC50 values as low as 0.50 μM. The NS3 helicase has been identified as a possible target of inhibition for several of these compounds, while the remaining inhibitors act via an undetermined mechanism. Gel shift assays suggest that helicase inhibition is a direct result of inhibitor-enzyme binding as opposed to direct RNA binding, and the ATPase activity of NS  ...[more]

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