Use of CID/ETD mass spectrometry to analyze glycopeptides

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Abstract

Collision-induced dissociation (CID) tandemmass spectrometry (MS/MS) does not allow the characterization of glycopeptides because of the fragmentation of glycan structures and limited fragmentation of peptide backbones. Electron transfer dissociation (ETD) MS/MS, on the other hand, offers a complementary approach, prompting only peptide backbone fragmentation while keeping post-translational modifications intact. Characterization of glycopeptides using both CID and ETD is summarized in this unit. While CID provides information related to the composition of glycan moieties attached to a peptide backbone, ETD permits de novo sequencing of peptides. Radical anion transfer of electrons to the peptide backbone in ETD induces cleavage of the N-Cα bond. The glycan moiety is retained on the peptide backbone, largely unaffected by the ETD process, thus allowing the identification of the amino acid sequence of a glycopeptide and its glycosylation site. This unit discusses the use of both CID and ETD for better characterization of glycopeptides.

Original languageEnglish
Article number12.11
JournalCurrent Protocols in Protein Science
Volume1
Issue numberSUPPL.68
DOIs
StatePublished - Apr 2012

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Keywords

  • CID
  • ETD
  • Glycopeptides
  • Glycoproteins
  • Tandem mass spectrometry

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