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A simple method to differentiate underivatized diastereomeric hexosamine monosaccharides, glucosamine, galactosamine, and mannosamine is reported by applying the kinetic method using N-acetylhexosamines or naturally occurring amino acids as reference bases under electrospray ionization conditions. The observed differences to distinguish the diastereomeric hexosamines are found mainly due to the proton affinity (PA) differences between the analyte and the reference base. The PA values of the hexosamines are not available in the literature, and hence, we estimated them by the kinetic method using N-acetylhexosamines as reference bases. The determined PA values are 223.97 kcal/mol for glucosamine, 224.99 kcal/mol for mannosamine, and 224.71 kcal/mol for galactosamine. The similar PA values were also obtained by using amino acids as reference bases. We have applied the same methodology to quantify these hexosamines in a mixture following the three-point calibration method suggested in the literature.

The DNA tetranucleotides, extended versions of GCA at the 3'-end or 5'-end, were used as chiral selectors for the chiral discrimination of atenolol, DOPA, tamsulosin, valacyclovir and zolmitriptan. Chiral discrimination was achieved by investigating the collision-induced dissociation spectra of the [X+Y-2H](2-) ion generated by electrospraying a solution mixture of tetranucleotide (X) and R- or S-analyte drug (Y). The relative abundances of the precursor ion and the product ion, resulting from the loss of drug, were considered for measuring the degree of chiral discrimination. Among all the tetranucleotides studied, AGCA showed the highest chiral discrimination. The present study emphasised the position of an adenine base in the tetranucleotide in chiral discrimination. The suitability of the method for the measurement of optical purity was also demonstrated in the case of zolmitriptan.

Protein-ligand interactions were studied for bovine insulin-amino sugar systems under electrospray ionisation mass spectrometry conditions. The isomeric amino sugars showed differences in the relative abundance of 1:1 protein-ligand complex formation. The electrospray ionisation and tandem mass spectrometry results of the complex clearly demonstrated that the differences in the interaction of isomeric sugars with insulin are mainly due to the differences in their gas-phase basicity. The same phenomenon is replicated in the formation of complexes between insulin and other ligands, such as amino acids, as well as in the binding of the amino sugars with amyloid β 1-40 peptide.

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