Characterization of mycosporine-serine-glycine methyl ester, a major mycosporine-like amino acid from dinoflagellates: a mass spectrometry study

Authors

  • Mario O. Carignan,

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    • Instituto Nacional de Investigación y Desarrollo Pesquero, Mar del Plata, Argentina
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  • José I. Carreto

    1. Instituto Nacional de Investigación y Desarrollo Pesquero, Mar del Plata, Argentina
    2. Departamento de Ciencias Marinas, FCEyN, Universidad Nacional de Mar del Plata, Mar del Plata, Argentina
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Address for correspondence: e-mail marioc@inidep.edu.ar.

Abstract

Several unknown mycosporine-like amino acids (MAAs) have been previously isolated from some cultured species of toxic dinoflagellates of the Alexandrium genus (Dinophyceae). One of them, originally called M-333, was tentatively identified as a shinorine methyl ester, but the precise nature of this compound is still unknown. Using a high-resolution reversed-phase liquid chromatography mass spectrometry analyses (HPLC/MS), we found that natural populations of the red tide dinoflagellate Prorocentrum micans Ehrenberg showed a net dominance of M-333 together with lesser amounts of other MAAs. We also documented the isolation and characterization of this MAA from natural dinoflagellate populations and from Alexandrium tamarense (Lebour) Balech cultures. Using a comparative fragmentation study in electrospray mass spectrometry between deuterated and non-deuterated M-333 compounds and synthesized mono and dimethyl esters of shinorine, this novel compound was characterized as mycosporine-serine-glycine methyl ester, a structure confirmed by nuclear magnetic resonance. These isobaric compounds can be differentiated by their fragmentation patterns in MS3 experiments because the extension and the specific site of the methylation changed the fragmentation pathway.

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