- Results as:
- Print view
- Endnote (RIS)
- BibTeX
- Table: CSV | HTML
Publications
Research Mission and Profile
Molecular Signal Processing
Bioorganic Chemistry
Biochemistry of Plant Interactions
Cell and Metabolic Biology
Independent Junior Research Groups
Program Center MetaCom
Publications
Good Scientific Practice
Research Funding
Networks and Collaborative Projects
Symposia and Colloquia
Alumni Research Groups
Publications
Glycation is referred to as the interaction of protein amino and guanidino groups with reducing sugars and carbonyl products of their degradation. Resulting advanced glycation end-products (AGEs) contribute to pathogenesis of diabetes mellitus and neurodegenerative disorders. Upon their intestinal absorption, dietary sugars and á-dicarbonyl compounds interact with blood proteins yielding AGEs. Although the differences in glycation potential of monosaccharides are well characterized, the underlying mechanisms are poorly understood. To address this question, D-glucose, D-fructose and L-ascorbic acid were incubated with human serum albumin (HSA). The sugars and á-dicarbonyl intermediates of their degradation were analyzed in parallel to protein glycation patterns (exemplified with hydroimidazolone modifications of arginine residues and products of their hydrolysis) by bottom-up proteomics and computational chemistry. Glycation of HSA with sugars revealed 9 glyoxal- and 14 methylglyoxal-derived modification sites. Their dynamics was sugar-specific and depended on concentrations of á-dicarbonyls, their formation kinetics, and presence of stabilizing residues in close proximity to the glycation sites.