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J Am Soc Mass Spectrom. 2014 Apr;25(4):673-83. doi: 10.1007/s13361-013-0799-2. Epub 2014 Jan 28.

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

Author information

1
Warwick Centre for Analytical Science, Department of Chemistry, University of Warwick, Coventry, UK.

Abstract

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.

PMID:
24470193
DOI:
10.1007/s13361-013-0799-2
[Indexed for MEDLINE]

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