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 language | English |
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Pages (from-to) | 673-683 |
Number of pages | 11 |
Journal | Journal of the American Society for Mass Spectrometry |
Volume | 25 |
Issue number | 4 |
Early online date | 28 Jan 2014 |
DOIs | |
Publication status | Published - 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