The binding of okadaic acid analogs to recombinant OABP2.1 originally isolated from the marine sponge Halichondria okadai

Keiichi Konoki, Tatsuya Onoda, Sachie Furumochi, Yuko Cho, Mari Yotsu-Yamashita, Takeshi Yasumoto

    Research output: Contribution to journalArticlepeer-review

    4 Citations (Scopus)

    Abstract

    The binding between [24-3H]okadaic acid (OA) and a recombinant OA binding protein OABP2.1 was examined using various OA analog, including methyl okadaate, norokadanone, 7-deoxy OA, and 14,15-dihydro OA, 7-O-palmitoyl DTX1, to investigate the structure activity relationship. Among them, 7-O-palmitoyl DTX1, which is one of the diarrhetic shellfish poisoning (DSP) toxins identified in shellfish, displayed an IC50 for [24- 3H]OA binding at 51 ± 6.3 nM (Mean ± SD). In addition, a synthetic compound, N-pyrenylmethyl okadamide, exhibited its IC50 at 10 ± 2.9 nM (Mean ± SD). These results suggested that the recombinant OABP2.1 and the N-pyrenylmethyl okadamide might be core substances in a novel assay for the DSP toxins.

    Original languageEnglish
    Pages (from-to)5833-5835
    Number of pages3
    JournalBioorganic and Medicinal Chemistry Letters
    Volume23
    Issue number21
    DOIs
    Publication statusPublished - 2013 Nov 1

    Keywords

    • Diarrhetic shellfish poisoning
    • Dinophysistoxins
    • Okadaic acid
    • Okadaic acid binding protein

    ASJC Scopus subject areas

    • Biochemistry
    • Molecular Medicine
    • Molecular Biology
    • Pharmaceutical Science
    • Drug Discovery
    • Clinical Biochemistry
    • Organic Chemistry

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