Unexpected crosslinking and diglycation as advanced glycation end-products from glyoxal

Andrea F. Lopez-Clavijo, Carlos A. Duque-Daza, Andrew Soulby, Isolda Romero Canelon, Mark Barrow, Peter B. O'Connor

Research output: Contribution to journalArticlepeer-review

6 Citations (Scopus)


Glyoxal-derived advanced glycation end-products (AGEs) are formed in physiological systems affecting protein/peptide function and structure. These AGEs are generated during aging and chronic diseases such as diabetes and are considered arginine glycating agents. Thus, the study of glyoxal-derived AGEs in lysine residues and amino acid competition is addressed here using acetylated and non-acetylated undecapeptides, with one arginine and one lysine residue available for glycation. Tandem mass spectrometry results from a Fourier transform ion cyclotron resonance mass spectrometer showed glycated species at both the arginine and lysine residues. One species with the mass addition of 116.01096 Da is formed at the arginine residue. A possible structure is proposed to explain this finding (Nδ-[2-(dihydroxymethyl)-2H,3aH,4H,6aH-[1, 3]dioxolo[5,6-d]imidazolin-5-yl]-L-ornithine-derived AGE). The second species corresponded to intramolecular crosslink involving the lysine residue and its presence is checked with ion-mobility mass spectrometry.

Original languageEnglish
Pages (from-to)2125-2133
Number of pages9
JournalJournal of the American Society for Mass Spectrometry
Issue number12
Publication statusPublished - Dec 2014


  • Advanced glycation endproducts (AGEs)
  • AGEs crosslinking
  • CAD
  • CID
  • Collisionally activated dissociation
  • ECD
  • Electron capture dissociation
  • Glycation
  • Glyoxal
  • Maillard reaction
  • Mass spectrometry
  • PTMs

ASJC Scopus subject areas

  • Structural Biology
  • Spectroscopy


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