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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