The IPB has once again been recognized for its exemplary actions in terms of equal opportunity-oriented personnel and organizational policies and has received the TOTAL E-QUALITY certification for the…
The Plant Science Student Conference (PSSC) has been organised by students from the two Leibniz institutes, IPK and IPB, every year for the last 20 years. In this interview, Christina Wäsch (IPK) and…
Frolova, N.; Soboleva, A.; Nguyen, V. D.; Kim, A.; Ihling, C.; Eisenschmidt-Bönn, D.; Mamontova, T.; Herfurth, U. M.; Wessjohann, L. A.; Sinz, A.; Birkenmeyer, C.; Frolov, A.;Probing glycation potential of dietary sugars in human blood by anintegrated in vitro approachFood Chem.347128951(2021)DOI: 10.1016/j.foodchem.2020.128951
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.