Format

Send to

Choose Destination
See comment in PubMed Commons below
Bioorg Med Chem Lett. 2014 Jan 15;24(2):609-12. doi: 10.1016/j.bmcl.2013.12.012. Epub 2013 Dec 9.

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

Author information

1
Department of Chemistry and Biochemistry, University of Maryland, Baltimore County, 1000 Hilltop Circle, Baltimore, MD 21250, United States.
2
Department of Molecular Biology, John Paul II Catholic University of Lublin, Poland.
3
Department of Chemistry and Biochemistry, University of Maryland, Baltimore County, 1000 Hilltop Circle, Baltimore, MD 21250, United States. Electronic address: pjsmith@umbc.edu.

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 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 NS3 is not affected. The syntheses and biological results are presented herein.

KEYWORDS:

Helicase; Hepatitis C; Inhibitor; NS3

PMID:
24360997
DOI:
10.1016/j.bmcl.2013.12.012
[Indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science
    Loading ...
    Support Center