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

Bioorg Med Chem Lett. 2013 Nov 1;23(21):5833-5. doi: 10.1016/j.bmcl.2013.08.099. Epub 2013 Sep 6.

Abstract

The binding between [24-(3)H]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-(3)H]OA binding at 51±6.3nM (Mean±SD). In addition, a synthetic compound, N-pyrenylmethyl okadamide, exhibited its IC50 at 10±2.9nM (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.

Keywords: Diarrhetic shellfish poisoning; Dinophysistoxins; Okadaic acid; Okadaic acid binding protein.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Marine Toxins / chemistry*
  • Marine Toxins / metabolism*
  • Okadaic Acid / analogs & derivatives*
  • Okadaic Acid / metabolism*
  • Porifera / chemistry
  • Porifera / metabolism*
  • Protein Binding
  • Recombinant Proteins / metabolism

Substances

  • Marine Toxins
  • Recombinant Proteins
  • Okadaic Acid