Gln-Gly cleavage: a dominant dissociation site in the fragmentation of protonated peptides

Rapid Communications in Mass Spectrometry : RCM
A P JonssonW J Griffiths

Abstract

An understanding of the gas-phase dissociation of protonated peptides within the mass spectrometer is essential for automated high-throughput protein identification. In this communication we describe a facile cleavage of the Gln-Gly peptide bond under low-collisional energy conditions. A variety of synthetic peptides have been analysed where key amino acids have been substituted within the sequence PQGPPQQGGR, which is a consensus repeat present in the tryptic peptides of acidic proline-rich protein 1 (PRP-1). The collision-induced dissociation spectra obtained from the PRP-1 tryptic peptides and the synthetic peptides indicate that facile Gln-Gly cleavage occurs when an X-Gln-Gly-Y sequence is present in a peptide, where X is any amino acid and Y any amino acid other than Gly.

References

Sep 1, 1986·Proceedings of the National Academy of Sciences of the United States of America·D F HuntC R Hauer
Nov 1, 1984·Biomedical Mass Spectrometry·P Roepstorff, J Fohlman
Oct 23, 1998·Science·F S CollinsL Walters
Dec 13, 2000·Rapid Communications in Mass Spectrometry : RCM·Y WangW J Griffiths
Apr 3, 2001·Journal of the American Society for Mass Spectrometry·A P JonssonN Strömberg

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Citations

Aug 5, 2006·Biophysical Chemistry·Grazyna StrzelczakKrzysztof Bobrowski
Aug 28, 2001·Journal of Mass Spectrometry : JMS
Sep 25, 2004·Mass Spectrometry Reviews·Béla Paizs, Sándor Suhai

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