Study of an unusual advanced glycation end-product (AGE) derived from glyoxal using mass spectrometry.
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.
Warwick Centre for Analytical Science, Department of Chemistry, University of Warwick, Coventry, UK.
Andrea F
AF
Lopez-Clavijo
Carlos A
CA
Duque-Daza
Isolda
I
Romero Canelon
Mark P
MP
Barrow
David
D
Kilgour
Naila
N
Rabbani
Paul J
PJ
Thornalley
Peter B
PB
O'Connor
D017127:Glycation End Products, Advanced / Q000032:analysis* / Q000737:chemistry*; D006031:Glycosylation; D006037:Glyoxal / Q000737:chemistry*; D010455:Peptides / Q000032:analysis / Q000737:chemistry; D053719:Tandem Mass Spectrometry / Q000379:methods*
D017127:Glycation End Products, Advanced; D010455:Peptides; D006037:Glyoxal