The role of proton mobility in determining the energy-resolved vibrational activation/dissociation channels of N-glycopeptide ions

Venkata Kolli, Heidi A. Roth, Gabriela De La Cruz, Ganga S. Fernando, Eric D Dodds

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Site-specific glycoproteomic analysis largely hinges on the use of tandem mass spectrometry (MS/MS) to identify glycopeptides. Experiments of this type are usually aimed at drawing connections between individual oligosaccharide structures and their specific sites of attachment to the polypeptide chain. These determinations inherently require ion dissociation methods capable of interrogating both the monosaccharide and amino acid connectivity of the glycopeptide. Collision-induced dissociation (CID) shows potential to satisfy this requirement, as the vibrational activation/dissociation of protonated N-glycopeptides has been observed to access cleavage of either glycosidic bonds of the glycan or amide bonds of the peptide in an energy-resolved manner. Nevertheless, the relative energy requirement for these fragmentation pathways varies considerably among analytes. This research addresses the influence of proton mobility on the vibrational energy necessary to achieve either glycan or peptide cleavage in a collection of protonated N-glycopeptide ions. While greater proton mobility of the precursor ion was found to correlate with lower energy requirements for precursor ion depletion and appearance of glycosidic fragments, the vibrational energy deposition necessary for appearance of peptide backbone fragments showed no relation to the precursor ion proton mobility. These results are consistent with observations suggesting that peptide fragments arise from an intermediate fragment which is generally of lower proton mobility than the precursor ion. Such findings have potential to facilitate the rational selection of CID conditions which are best suited to provide either glycan or peptide cleavage products in MS/MS based N-glycoproteomic analysis.

Original languageEnglish (US)
Pages (from-to)85-92
Number of pages8
JournalAnalytica Chimica Acta
Volume896
DOIs
StatePublished - Oct 8 2015

Fingerprint

Glycopeptides
Protons
peptide
Chemical activation
Ions
ion
cleavage
Polysaccharides
energy
Peptides
Peptide Fragments
collision
monosaccharide
Monosaccharides
Hinges
Tandem Mass Spectrometry
Oligosaccharides
Amides
Mass spectrometry
connectivity

Keywords

  • Collision-induced dissociation
  • Glycopeptides
  • Glycoproteins
  • Glycoproteomics
  • Proton mobility
  • Tandem mass spectrometry

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry
  • Environmental Chemistry
  • Spectroscopy

Cite this

The role of proton mobility in determining the energy-resolved vibrational activation/dissociation channels of N-glycopeptide ions. / Kolli, Venkata; Roth, Heidi A.; De La Cruz, Gabriela; Fernando, Ganga S.; Dodds, Eric D.

In: Analytica Chimica Acta, Vol. 896, 08.10.2015, p. 85-92.

Research output: Contribution to journalArticle

Kolli, Venkata ; Roth, Heidi A. ; De La Cruz, Gabriela ; Fernando, Ganga S. ; Dodds, Eric D. / The role of proton mobility in determining the energy-resolved vibrational activation/dissociation channels of N-glycopeptide ions. In: Analytica Chimica Acta. 2015 ; Vol. 896. pp. 85-92.
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