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

    4 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

    Fingerprint

    Halogenated Diphenyl Ethers
    hepatitis
    Hepatitis Viruses
    viruses
    Viruses
    ethers
    proteins
    Adenosine Triphosphatases
    Proteins
    RNA Helicases
    Bromine
    Porifera
    Structure-Activity Relationship
    bromine
    Benzene
    Scaffolds
    Hepacivirus
    Hydroxyl Radical
    inhibitors
    Antiviral Agents

    Keywords

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

    ASJC Scopus subject areas

    • Organic Chemistry
    • Medicine(all)

    Cite this

    Salam, K. A., Furuta, A., Noda, N., Tsuneda, S., Sekiguchi, Y., Yamashita, A., ... 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

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

    In: Molecules, Vol. 19, No. 4, 2014, p. 4006-4020.

    Research output: Contribution to journalArticle

    Salam, KA, Furuta, A, Noda, N, Tsuneda, S, Sekiguchi, Y, Yamashita, A, Moriishi, K, Nakakoshi, M, Tani, H, Roy, SR, Tanaka, J, Tsubuki, M & Akimitsu, N 2014, 'PBDE: Structure-activity studies for the inhibition of hepatitis c virus ns3 helicase' Molecules, vol. 19, no. 4, pp. 4006-4020. https://doi.org/10.3390/molecules19044006
    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. / PBDE : Structure-activity studies for the inhibition of hepatitis c virus ns3 helicase. In: Molecules. 2014 ; Vol. 19, No. 4. pp. 4006-4020.
    @article{45844db4c1ec47dc8ece35936c136b5f,
    title = "PBDE: Structure-activity studies for the inhibition of hepatitis c virus ns3 helicase",
    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, Marine sponge, NS3 RNA helicase, Polybrominated diphenyl ether",
    author = "Salam, {Kazi Abdus} and Atsushi Furuta and Naohiro Noda and Satoshi Tsuneda and Yuji Sekiguchi and Atsuya Yamashita and Kohji Moriishi and Masamichi Nakakoshi and Hidenori Tani and Roy, {Sona Rani} and Junichi Tanaka and Masayoshi Tsubuki and Nobuyoshi Akimitsu",
    year = "2014",
    doi = "10.3390/molecules19044006",
    language = "English",
    volume = "19",
    pages = "4006--4020",
    journal = "Molecules",
    issn = "1420-3049",
    publisher = "Multidisciplinary Digital Publishing Institute (MDPI)",
    number = "4",

    }

    TY - JOUR

    T1 - PBDE

    T2 - Structure-activity studies for the inhibition of hepatitis c virus ns3 helicase

    AU - Salam, Kazi Abdus

    AU - Furuta, Atsushi

    AU - Noda, Naohiro

    AU - Tsuneda, Satoshi

    AU - Sekiguchi, Yuji

    AU - Yamashita, Atsuya

    AU - Moriishi, Kohji

    AU - Nakakoshi, Masamichi

    AU - Tani, Hidenori

    AU - Roy, Sona Rani

    AU - Tanaka, Junichi

    AU - Tsubuki, Masayoshi

    AU - Akimitsu, Nobuyoshi

    PY - 2014

    Y1 - 2014

    N2 - 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.

    AB - 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.

    KW - Hepatitis C virus

    KW - Marine sponge

    KW - NS3 RNA helicase

    KW - Polybrominated diphenyl ether

    UR - http://www.scopus.com/inward/record.url?scp=84899504908&partnerID=8YFLogxK

    UR - http://www.scopus.com/inward/citedby.url?scp=84899504908&partnerID=8YFLogxK

    U2 - 10.3390/molecules19044006

    DO - 10.3390/molecules19044006

    M3 - Article

    VL - 19

    SP - 4006

    EP - 4020

    JO - Molecules

    JF - Molecules

    SN - 1420-3049

    IS - 4

    ER -