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.
Highlights
C Virus nonstructural protein 3 (NS3) HelicaseKazi Abdus Salam 1, Atsushi Furuta 2,3, Naohiro Noda 2,3, Satoshi Tsuneda 2, Yuji Sekiguchi 3, Atsuya Yamashita 4, Kohji Moriishi 4, Masamichi Nakakoshi 5, Hidenori Tani 6, Sona Rani Roy 7, Junichi Tanaka 7, Masayoshi Tsubuki 8,* and Nobuyoshi Akimitsu 1,*
Hepatitis C virus (HCV) is one of the major causative agents for hepatitis C, which has caused an epidemic of liver fibrosis, cirrhosis, and hepatocellular carcinoma [1]
To screen potential nonstructural protein 3 (NS3) helicase inhibitors from extracts of marine organisms, we used a highthroughput fluorescence helicase assay based on FRET [23]
Summary
Kazi Abdus Salam 1, Atsushi Furuta 2,3, Naohiro Noda 2,3, Satoshi Tsuneda 2, Yuji Sekiguchi 3, Atsuya Yamashita 4, Kohji Moriishi 4, Masamichi Nakakoshi 5, Hidenori Tani 6, Sona Rani Roy 7, Junichi Tanaka 7, Masayoshi Tsubuki 8,* and Nobuyoshi Akimitsu 1,*. Research Institute for Environmental Management Technology, National Institute of Advanced. Received: 17 January 2014; in revised form: 5 March 2014 / Accepted: 13 March 2014 /
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