Differentiation of free d-amino acids and amino acid isomers in solution using tandem mass spectrometry of hydrogen-bonded clusters

Abstract

Free d-amino acids and amino acid isomers were differentiated using tandem mass spectrometry without chromatographic separation. Ultraviolet photodissociation and water adsorption of leucine (Leu) and isoleucine (Ile) enantiomers hydrogen-bonded with tryptophan (Trp) were investigated at 8 K in the gas phase. The enantiomer-selective Cα–Cβ bond cleavage of Trp was observed in the product ion spectra obtained by 285 nm photoexcitation, where the abundance of NH2CHCOOH-eliminated ion of heterochiral H+(d-Trp)(l-Leu) was higher than that of homochiral H+(l-Trp)(l-Leu). When comparing water adsorption on the surfaces of the heterochiral and homochiral clusters in a cold ion trap, the number of water molecules adsorbed on the heterochiral cluster was greater than that adsorbed on the homochiral cluster. These results indicate that the stronger intermolecular interactions within the homochiral H+(l-Trp)(l-Leu) compared to the heterochiral cluster inhibit enantiomer-selective photodissociation. Leu and Ile were differentiated by the isomer-selective Cα–Cβ bond cleavage of Trp in the clusters. Calibration curves for the differentiation of isomeric amino acids and their enantiomers were developed using monitoring isomer- and enantiomer-selective photodissociation, indicating that the molar fractions in solution could be determined from a single product ion spectrum.