Gln-Gly cleavage: Correlation between collision-induced dissociation and biological degradation |
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Authors: | Andreas P. Jonsson Tomas Bergman Hans Jörnvall William J. Griffiths Per Bratt Nicklas Strömberg |
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Affiliation: | Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden. andreas.jonsson@mbb.ki.se |
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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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