Monosaccharides interact weakly with human serum albumin. Insights for the functional perturbations on the binding capacity of albumin. (March 2021)

• Record Type: Journal Article
• Authors: Chaves, Otávio A.; Soares, Marilia A.G.; Campos de Oliveira, Márcia Cristina
• Is Part Of: Carbohydrate research. Volume 501(2021)
• Publication Date: 2021-03
• Subjects: Glucose -- Fructose -- Arabinose -- Spectroscopy -- HSA-Binding -- Molecular docking; Carbohydrates -- Periodicals; Chemistry, Organic -- Periodicals; Biochemistry -- Periodicals; Carbohydrates -- Periodicals; Chimie organique -- Périodiques; Glucides -- Périodiques; Biochemistry; Carbohydrates; Chemistry, Organic; Periodicals; Electronic journals; 507.78
• DOI: 10.1016/j.carres.2021.108274
• Languages: English
• ISSNs: 0008-6215

Abstract

Abstract: Monosaccharides, e.g. fructose, glucose, and arabinose are present in most foods consumed daily, whether, in natural or industrialized forms, and their concentration in the human bloodstream can impact the formation of advanced glycation end-products (AGEs, prevalent in people with diabetes) impacting the profile of Human Serum Albumin (HSA) in biodistribution of endogenous and exogenous compounds. Multiple spectroscopic techniques (UV–vis, circular dichroism, steady-state, and time-resolved fluorescence) combined with molecular docking showed that carbohydrates interact weakly and spontaneously via a ground-state association with HSA. The binding is enthalpically and entropically driven in the subdomain IIA (site I) and perturb weakly the secondary structure of the albumin. Hydrogen bonding and van der Waals forces are the main intermolecular interactions involved in the ligand binding, as well as hydrophobic effects related to the release of hydration shell upon ligand binding. Overall, the results indicated that an increase in glucose, fructose or arabinose level in the human bloodstream may cause functional perturbation on the binding capacity of albumin. Therefore, there is the necessity of carbohydrate level control in the bloodstream to not compromise the interaction and distribution of exogenous and endogenous compounds by HSA. Graphical abstract: Image 1 Highlights: Fructose, glucose, and arabinose interact weakly with human serum albumin (HSA), being enthalpically and entropically driven. The monosaccharides do not perturb significantly the secondary structure of the protein. There is a ground-state association between HSA and monosaccharides into site I (subdomain IIA). Fructose, glucose, and arabinose might cause functional perturbation on the binding capacity of albumin.