TY - JOUR

T1 - Probing glycation potential of dietary sugars in human blood by an integrated in vitro approach

AU - Фролова, Надежда Владимировна

AU - Соболева, Алена Вадимовна

AU - Нгуен, Вьет Дук

AU - Ким, Айонг

AU - Илинг, Кристиан

AU - Айзеншмидт-Бённ, Даниела

AU - Мамонтова, Татьяна

AU - Херфурт, Ута Мария

AU - Вессйоханн, Лудгер А.

AU - Зинц, Андреа

AU - Биркемайер, Клаудиа

AU - Фролов, Андрей Александрович

N1 - Publisher Copyright: © 2020 Elsevier Ltd

PY - 2021/6/15

Y1 - 2021/6/15

N2 - 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.

AB - 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.

KW - Advanced glycation end products (AGEs)α-Dicarbonyl compoundsBlood monosaccharidesGC–MSGlycationGlyoxal (GO)LC–MSMethylglyoxal (MGO)

KW - Advanced glycation end products (AGEs)

KW - Blood monosaccharides

KW - GC–MS

KW - Glycation

KW - Glyoxal (GO)

KW - LC–MS

KW - Methylglyoxal (MGO)

KW - α-Dicarbonyl compounds

KW - GC-MS

KW - LC-MS

KW - alpha-Dicarbonyl compounds

UR - https://www.sciencedirect.com/science/article/abs/pii/S0308814620328338

UR - https://doi.org/10.1016/j.foodchem.2020.128951

UR - http://www.scopus.com/inward/record.url?scp=85099678264&partnerID=8YFLogxK

UR - https://www.mendeley.com/catalogue/be729f70-247c-3c3b-9afa-28c93ace211f/

U2 - 10.1016/j.foodchem.2020.128951

DO - 10.1016/j.foodchem.2020.128951

M3 - Article

C2 - 33493836

VL - 347

JO - Food Chemistry

JF - Food Chemistry

SN - 0308-8146

M1 - 128951

ER -