Fragmentation characteristics of glycopeptides

Károly Vékey, Oliver Ozohanics, Eszter Tóth, Anita Jek, Ágnes Révész, Judit Krenyácz, László Drahos

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

Mass spectrometric analysis of glycopeptides is an emerging strategy for analysis of glycosylation patterns. Here we present an approach using energy resolved collision induced dissociation (CID) spectra to determine structural features of glycopeptides. Fragmentation of multiply protonated glycopeptides proceeds by a series of competing charge separation processes by cleavage of a glycosidic bond, each producing two charged products: a singly charged, "B" type sugar (oxonium) ion, and a complementary high mass fragment. Energy requirements (activation energies) of these processes are similar to each other, and are far less, than that required for peptide fragmentation. At higher collision energies these first generation products fragment further, yielding a complex fragmentation pattern. Analysis of low energy spectra (those corresponding to ca. 50% survival yield) are straightforward; the ions observed correspond to structural features present in the oligosaccharide, and are not complicated by consecutive reactions. This makes it feasible to identify and distinguish antenna- and core-fucosylated isomers; antenna fucosylation usually suggests presence of the Lewis-X antigen. In general, analysis of the triply protonated molecules are most advantageous, where neutral losses and monosaccharide oxonium ion formation are less abundant.

Original languageEnglish
Pages (from-to)71-79
Number of pages9
JournalInternational Journal of Mass Spectrometry
Volume345-347
DOIs
Publication statusPublished - Jul 1 2013

Keywords

  • Alpha-1-glycoprotein (AGP)
  • Cetuximab
  • Energy resolved mass spectra
  • Fucosylation
  • Glycosylation
  • Transferrin

ASJC Scopus subject areas

  • Instrumentation
  • Condensed Matter Physics
  • Spectroscopy
  • Physical and Theoretical Chemistry

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