Unexpected Crosslinking and Diglycation as Advanced Glycation End-Products from Glyoxal

• Published in: Journal of the American Society for Mass Spectrometry Vol. 25; no. 12; pp. 2125 - 2133
• Main Authors: Lopez-Clavijo, Andrea F., Duque-Daza, Carlos A., Soulby, Andrew, Canelon, Isolda Romero, Barrow, Mark, O’Connor, Peter B.
• Format: Journal Article
• Language: English
• Published: Boston Springer US 01-12-2014; Springer Nature B.V
• Subjects: Age; Amino Acid Sequence; Analytical Chemistry; Bioinformatics; Biotechnology; Chemistry; Chemistry and Materials Science; Cross-Linking Reagents - chemistry; Cross-Linking Reagents - metabolism; Crosslinking; Cyclotron resonance; Diabetes mellitus; Fourier transforms; Glycation End Products, Advanced - chemistry; Glycation End Products, Advanced - metabolism; Glycosylation; Glyoxal - chemistry; Glyoxal - metabolism; Ionic mobility; Ions; Lysine; Lysine - chemistry; Mass Spectrometry; Organic Chemistry; Peptides - chemistry; Peptides - metabolism; Proteomics; Research Article; Residues; Scientific imaging; Spectroscopy; Electron capture dissociation; AGEs crosslinking; ECD; CAD; Maillard reaction; Collisionally activated dissociation; Glyoxal; Mass spectrometry; Glycation; Advanced glycation endproducts (AGEs); PTMs; CID
• ISSN: 1044-0305; 1879-1123
• DOI: 10.1007/s13361-014-0996-7

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.
Graphical Abstract
ᅟ