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Molecules 2014, 19(4), 4006-4020; doi:10.3390/molecules19044006
Article

PBDE: Structure-Activity Studies for the Inhibition of Hepatitis C Virus NS3 Helicase

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Received: 17 January 2014 / Revised: 5 March 2014 / Accepted: 13 March 2014 / Published: 2 April 2014
(This article belongs to the Section Metabolites)
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Abstract

The helicase portion of the hepatitis C virus nonstructural protein 3 (NS3) is considered one of the most validated targets for developing direct acting antiviral agents. We isolated polybrominated diphenyl ether (PBDE) 1 from a marine sponge as an NS3 helicase inhibitor. In this study, we evaluated the inhibitory effects of PBDE (1) on the essential activities of NS3 protein such as RNA helicase, ATPase, and RNA binding activities. The structure-activity relationship analysis of PBDE (1) against the HCV ATPase revealed that the biphenyl ring, bromine, and phenolic hydroxyl group on the benzene backbone might be a basic scaffold for the inhibitory potency.
Keywords: hepatitis C virus; NS3 RNA helicase; marine sponge; polybrominated diphenyl ether hepatitis C virus; NS3 RNA helicase; marine sponge; polybrominated diphenyl ether
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Salam, K.A.; Furuta, A.; Noda, N.; Tsuneda, S.; Sekiguchi, Y.; Yamashita, A.; Moriishi, K.; Nakakoshi, M.; Tani, H.; Roy, S.R.; Tanaka, J.; Tsubuki, M.; Akimitsu, N. PBDE: Structure-Activity Studies for the Inhibition of Hepatitis C Virus NS3 Helicase. Molecules 2014, 19, 4006-4020.

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