Journal
RAPID COMMUNICATIONS IN MASS SPECTROMETRY
Volume 22, Issue 19, Pages 3027-3034Publisher
JOHN WILEY & SONS LTD
DOI: 10.1002/rcm.3703
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Funding
- NCRR NIH HHS [P41 RR018522-06, P41 RR018522, RR018522] Funding Source: Medline
- NIDDK NIH HHS [DK071283, R33 DK071283, R33 DK071283-04, R21 DK071283] Funding Source: Medline
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Non-enzymatic glycation of tissue proteins has important implications in the development of complications of diabetes mellitus. While electron transfer dissociation (ETD) has been shown to outperform collision-induced dissociation (CID) in sequencing glycated peptides by tandem mass spectrometry, ETD instrumentation is not yet widely available and often suffers from significantly lower sensitivity than CID. In this study, we evaluated different advanced CID techniques (i.e., neutral-loss-triggered MS3 and multi-stage activation) during liquid chromatography/multi-stage mass spectrometric (LC/MSn) analyses of Amadori-modified peptides enriched from human serum glycated in vitro. During neutral-loss-triggered MS3 experiments, MS3 scans triggered by neutral losses of 3 H2O or 3 H2O + HCHO produced similar results in terms of glycated peptide identifications. However, neutral losses of 3 H2O resulted in significantly more glycated peptide identifications during multi-stage activation experiments. Overall, the multi-stage activation approach produced more glycated peptide identifications, while the neutral-loss-triggered MS3 approach resulted in much higher specificity. Both techniques are viable alternatives to ETD for identifying glycated peptides. Copyright (c) 2008 John Wiley & Sons, Ltd.
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