Study of an unusual advanced glycation end-product (AGE) derived from glyoxal using mass spectrometry

Andrea F. Lopez-Clavijo, Carlos A. Duque-Daza, Isolda Romero Canelon, Mark P. Barrow, David Kilgour, Naila Rabbani, Paul J. Thornalley, Peter B. O'Connor

Research output: Contribution to journalArticlepeer-review

10 Citations (Scopus)

Abstract

(Chemical Presented) Glycation is a post-translational modification (PTM) that affects the physiological properties of peptides and proteins. In particular, during hyperglycaemia, glycation by α-dicarbonyl compounds generate α-dicarbonyl-derived glycation products also called α-dicarbonyl-derived advanced glycation end products. Glycation by the α-dicarbonyl compound known as glyoxal was studied in model peptides by MS/MS using a Fourier transform ion cyclotron resonance mass spectrometer. An unusual type of glyoxal-derived AGE with a mass addition of 21.98436 Da is reported in peptides containing combinations of two arginine-two lysine, and one arginine-three lysine amino acid residues. Electron capture dissociation and collisionally activated dissociation results supported that the unusual glyoxal-derived AGE is formed at the guanidino group of arginine, and a possible structure is proposed to illustrate the 21.9843 Da mass addition.

Original languageEnglish
Pages (from-to)673-683
Number of pages11
JournalJournal of the American Society for Mass Spectrometry
Volume25
Issue number4
Early online date28 Jan 2014
DOIs
Publication statusPublished - Apr 2014

Keywords

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

ASJC Scopus subject areas

  • Structural Biology
  • Spectroscopy

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