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Collision-Induced Dissociation of Citrullinated Peptide Anions.

Authors :
Steckel, Arnold
Papp, Dávid
Uray, Katalin
Schlosser, Gitta
Source :
Journal of the American Society for Mass Spectrometry. 8/2/2023, Vol. 34 Issue 8, p1569-1575. 7p.
Publication Year :
2023

Abstract

Peptide identification by positive electrospray ionization (ES+) tandem mass spectrometry (MS/MS) is a well-established strategy in proteomics. Several research groups reported the usefulness of negative electrospray ionization (ES−) for gaining complementary structural information on peptides and their post-translational modifications (PTM) compared to ES+. Fragmentation of citrullinated peptides has not been previously explored in ES–. In this study, 9 peptides containing citrulline residues were investigated in ES– by stepwise collision energy-dependent measurements on a QTOF instrument and a Q-Orbitrap instrument. Our results of high resolution and mass accuracy show the favored citrulline-selective loss of HNCO from these peptide precursors and their fragmentssimilarly to that in ES+along with y-NH3/z, c, c-NH3/b sequence ions. Loss of HNCO from citrullinated peptides in ES– and a proposed mechanism for the reaction have been described here for the first time. HNCO loss intensities from precursors were generally even higher than that in ES+. Interestingly, the most intense fragments corresponded to neutral losses from sequence ions while intact sequence ions were usually minor components of the spectra. High-intensity ions related to cleavages N-terminal to Asp and Glu residues that have been previously reported were also observed. On the other hand, a relatively high number of peaks were observed, possibly due to internal fragmentation and/or scrambling events. While (ES−) MS/MS spectra always require manual inspection and the annotation may be ambiguous, the favorable loss of HNCO and the preferable cleavage N-terminal to Asp residues can be used to differentiate between citrullinated/deamidated sequences. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
10440305
Volume :
34
Issue :
8
Database :
Academic Search Index
Journal :
Journal of the American Society for Mass Spectrometry
Publication Type :
Academic Journal
Accession number :
169768030
Full Text :
https://doi.org/10.1021/jasms.3c00044