@Article{IPB-449,
author = {Frolova, N. and Soboleva, A. and Nguyen, V. D. and Kim, A. and Ihling, C. and Eisenschmidt-Bönn, D. and Mamontova, T. and Herfurth, U. M. and Wessjohann, L. A. and Sinz, A. and Birkenmeyer, C. and Frolov, A.},
title = {{Probing glycation potential of dietary sugars in human blood by anintegrated in vitro approach}},
year = {2021},
pages = {128951},
journal = {Food Chem.},
doi = {10.1016/j.foodchem.2020.128951},
url = {https://doi.org/10.1016/j.foodchem.2020.128951},
volume = {347},
abstract = {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.}    
}