PBDE: Structure-activity studies for the inhibition of hepatitis c virus ns3 helicase

Kazi Abdus Salam, Atsushi Furuta, Naohiro Noda, Satoshi Tsuneda, Yuji Sekiguchi, Atsuya Yamashita, Kohji Moriishi, Masamichi Nakakoshi, Hidenori Tani, Sona Rani Roy, Junichi Tanaka, Masayoshi Tsubuki, Nobuyoshi Akimitsu

Research output: Contribution to journalArticle

5 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)4006-4020
Number of pages15
JournalMolecules
Volume19
Issue number4
DOIs
Publication statusPublished - 2014 Apr

Keywords

  • Hepatitis C virus
  • Marine sponge
  • NS3 RNA helicase
  • Polybrominated diphenyl ether

ASJC Scopus subject areas

  • Analytical Chemistry
  • Chemistry (miscellaneous)
  • Molecular Medicine
  • Pharmaceutical Science
  • Drug Discovery
  • Physical and Theoretical Chemistry
  • Organic Chemistry

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  • Cite this

    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. (2014). PBDE: Structure-activity studies for the inhibition of hepatitis c virus ns3 helicase. Molecules, 19(4), 4006-4020. https://doi.org/10.3390/molecules19044006