Abstract
Tryptic digestion of the 150-residue human acidic salivary proline-rich protein 1 (PRP-1) generated eight peptides, two of which corresponded to the N-terminal 30-residue segment. In each of the other six tryptic peptides, a consensus repeat with the structure PQGPPQQGG was present. A facile Gln-Gly cleavage between the second and the third residues of the repeat was observed during collision-induced dissociation experiments. We postulate possible mechanisms to account for this reactivity, involving attack on the peptidyl carbonyl group by the Gln sidechain. Significantly, the Gln-Gly cleavage has been shown to be biologically important in the bacterial degradation of PRPs in saliva, generating bacteria-binding Pro-Gln C-termini. We suggest a link between the gas-phase chemistry and the biochemical degradation of these molecules.
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Jonsson, A.P., Bergman, T., Jörnvall, H. et al. Gln-Gly cleavage: Correlation between collision-induced dissociation and biological degradation. J Am Soc Mass Spectrom 12, 337–342 (2001). https://doi.org/10.1016/S1044-0305(01)00210-0
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DOI: https://doi.org/10.1016/S1044-0305(01)00210-0