�-N-methylamino-L-alanine may be a risk factor for amyotrophic lateral sclerosis, Parkinson's and Alzheimer's disease.  Neuronal assays suggest that the BMAA/bicarbonate allows for the formation of a carbamate adduct that might produce structures capable of activating glutamate receptors. Present are the highlights of a NMR based structural characterization of BMAA/Bicarbonate interaction and the adduct formations.A systematic study of the structure of BMAA as a function of temperature, pH, and at close to physiological conditions the BMAA/bicarbonate adducts formation at varying BMAA/bicarbonate ratios was studied.  Two adducts coexists simultaneously with BMAA in solution and these adducts undergo an exchange between complex and free form BMAA on the NMR time scale. Though these results add to an additional dimension to the complexity of BMAA's neurotoxicity, it provides an opportunity to address the molecular level mechanism of BMAA: Bicarbonate adducts responsible for the function.

Structural characterization of L-β-methyl-amino-alanine bicarbonate interaction reveals co-existence and conformational equilibria of multiple complexes at physiological condition: A comprehensive NMR study

245th National Meeting (2013)

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