Abstract
Collisional activation of [M + H]+ parent ions from peptides of n amino acid residues may yield a rearrangement that involves loss of the C-terminal amino acid residue to produce (b n−1 + H2O) daughters. We have studied this reaction by a retrospective examination of the m/z spectra of two collections of data. The first set comprised 398 peptides from coat protein digests of a number of plant viruses by various enzymes, where conditions in the tryptic digests were chosen so as to produce many missed cleavages. In this case, a large effect was observed—323 (b n−1 + H2O) daughter ions (∼81%), including 185 (∼46%) “strong” decays with ratios (b n−1 + H2O)/(b n−1) > 1. The second set comprised 1200 peptides, all from tryptic digests, which were carried out under more stringent conditions, resulting in relatively few missed cleavages. Even here, 190 (b n−1 + H2O) ions (∼16%) were observed, including 87 (> 7%) “strong” decays, so the effect is still appreciable. The results suggest that the tendency for (b n−1 + H2O) ion formation is promoted by the protonated side chain of a non-C-terminal basic amino acid residue, in the order arginine ≫ lysine ≥ histidine, and that its (non-C-terminal) position is not critical. The results can be interpreted by a mechanism in which hydrogen bonding between the protonated side chain and the (n − 1) carbonyl oxygen facilitates loss of the C-terminal amino acid residue to give a product ion having a carboxyl group at the new C-terminus.
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Preliminary accounts of some of these measurements were given at the 12th Lake Louise Workshop on Tandem Mass Spectrometry, Alberta, Canada, 1999, and at the 52nd Annual Conference of the American Society for Mass Spectrometry, Nashville, Tennessee, USA, 2004.
Published online April 5, 2007
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She, YM., Krokhin, O., Spicer, V. et al. Formation of (b n−1 + H2O) ions by collisional activation of maldi-formed peptide [M + H]+ ions in a QqTOF mass spectrometer. J Am Soc Mass Spectrom 18, 1024–1037 (2007). https://doi.org/10.1016/j.jasms.2007.02.008
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DOI: https://doi.org/10.1016/j.jasms.2007.02.008