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

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...

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Detalles Bibliográficos
Autores principales: Salam, Kazi Abdus, Furuta, Atsushi, Noda, Naohiro, Tsuneda, Satoshi, Sekiguchi, Yuji, Yamashita, Atsuya, Moriishi, Kohji, Nakakoshi, Masamichi, Tani, Hidenori, Roy, Sona Rani, Tanaka, Junichi, Tsubuki, Masayoshi, Akimitsu, Nobuyoshi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2014
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6271602/
https://www.ncbi.nlm.nih.gov/pubmed/24699145
http://dx.doi.org/10.3390/molecules19044006
Descripción
Sumario: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.

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