Probing glycation potential of dietary sugars in human blood by an integrated in vitro approach. (15th June 2021)

• Record Type: Journal Article
• Authors: Frolova, Nadezhda; Soboleva, Alena; Nguyen, Viet Duc; Kim, Ahyoung; Ihling, Christian; Eisenschmidt-Bönn, Daniela; Mamontova, Tatiana; Herfurth, Uta M.; Wessjohann, Ludger A.; Sinz, Andrea; Birkemeyer, Claudia; Frolov, Andrej
• Is Part Of: Food chemistry. Volume 347(2021)
• Publication Date: 2021-06-15
• Subjects: Advanced glycation end products (AGEs) -- α-Dicarbonyl compounds -- Blood monosaccharides -- GC–MS -- Glycation -- Glyoxal (GO) -- LC–MS -- Methylglyoxal (MGO); Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2020.128951
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: Sugar glycation potential. Carbonyl and AGE site profiling. Factors affecting AGE dynamics. 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 α-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 α-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 α-dicarbonyls, their formation kinetics, and presence of stabilizing residues in close proximity to the glycation sites.