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• W2321848425 abstract "β-methylamino-l-alanine (BMAA) is a naturally occurring nonprotein amino acid originally discovered in cycad seeds and traditional foods of the Chamorro people of Guam. Recent research has implicated BMAA as a potential factor in neurodegenerative disease and described the production of BMAA in cyanobacteria, but conflicting results have complicated the interpretation of data. We hypothesized that the reactivity of BMAA with metal ions in the sample matrix and the formation of metal adducts in electrospray ionization mass spectrometry (MS) analysis confound results. Dilute solutions of TCA, MgCl(2), NaCl, CuCl(2), ZnCl(2) (0.01 M), or artificial ocean water (Instant Ocean, 3.5 g/L) reduced the signal attributable to the BMAA M + H(+) peak by 78-99.7%. The degree of adduct formation was significantly affected by MS settings such as induction voltage. A number of the detected ion peaks in BMAA standards were consistent with the formation of metal-BMAA complexes in addition to the adduct formation. A standard of Zn(BMAA)(2) was synthesized, and the effects of sample preparation, derivatization, column chromatography, pH, and interactions with serine were determined. Together, these data demonstrate that sample matrix, formation of adducts, and mass spectrometry settings complicate analysis of BMAA, that analysis by detection of the parent ion and daughter ion fragmentation patterns are highly susceptible to false negative findings, and that failure to detect BMAA cannot be considered proof of absence of the compound." @default.
• W2321848425 created "2016-06-24" @default.
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• W2321848425 date "2012-08-30" @default.
• W2321848425 modified "2023-10-13" @default.
• W2321848425 title "Reactivity of β-Methylamino-<scp>l</scp>-alanine in Complex Sample Matrixes Complicating Detection and Quantification by Mass Spectrometry" @default.
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• W2321848425 doi "https://doi.org/10.1021/ac301691r" @default.
• W2321848425 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22905767" @default.
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