Probing glycation potential of dietary sugars in human blood by an integrated in vitro approach.
Food Chem
; 347: 128951, 2021 Jun 15.
Article
em En
| MEDLINE
| ID: mdl-33493836
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.
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Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Açúcares da Dieta
/
Albumina Sérica Humana
Limite:
Humans
Idioma:
En
Ano de publicação:
2021
Tipo de documento:
Article