Details

Autor(en) / Beteiligte

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

Titel

Fragmentation characteristics of glycopeptides

Ist Teil von

• International journal of mass spectrometry, 2013-07, Vol.345-347, p.71-79

Ort / Verlag

Elsevier B.V

Erscheinungsjahr

2013

Link zum Volltext

Quelle

Elsevier ScienceDirect Journals Complete

Beschreibungen/Notizen

• [Display omitted] ► We present energy resolved CID spectra and fragmentation characteristics of glycopeptides. ► We suggest that glycopeptide analysis should be performed at low energy (SY50) to maximize information content. ► Possibility to determine fucosylation site based on MS/MS. 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.