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Characterization of mycosporine‐serine‐glycine methyl ester, a major mycosporine‐like amino acid from dinoflagellates: a mass spectrometry study
Author(s) -
Carignan Mario O.,
Carreto José I.
Publication year - 2013
Publication title -
journal of phycology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.85
H-Index - 127
eISSN - 1529-8817
pISSN - 0022-3646
DOI - 10.1111/jpy.12076
Subject(s) - dinoflagellate , biology , dinophyceae , serine , alexandrium tamarense , glycine , fragmentation (computing) , mass spectrometry , amino acid , biochemistry , chromatography , botany , algal bloom , chemistry , phytoplankton , enzyme , ecology , nutrient
Several unknown mycosporine‐like amino acids ( MAA s) have been previously isolated from some cultured species of toxic dinoflagellates of the A lexandrium 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 MAA s. We also documented the isolation and characterization of this MAA from natural dinoflagellate populations and from A lexandrium 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 MS 3 experiments because the extension and the specific site of the methylation changed the fragmentation pathway.