Abstract
AbstractIncreasing the degree of glycation in diabetes could affect the ability of plasma proteins in binding to small molecules and active compounds. In this study, the influence of glycation of Human serum albumin (HSA) on the binding affinities for six dietary flavonoids was investigated by fluorescence spectra. Glycated HSA was prepared through incubation with glucose and characterized by several methods to confirm the glycation. It was found that the level of glycation increased with the increasing incubation time. The glycation of HSA increased the binding affinities for flavonoids by 1.40 to 48.42 times, which indicates that modifications caused by the glycation may have different influences on the interactions of flavonoids with HSA at separate binding sites on this protein. These results are valuable for understanding the influence of diabetes on the metabolism of flavonoids and other bioactive small molecules in human body.
Highlights
Diabetes, which is known as diabetes mellitus, has become a big challenge in human health all over the world, and the prevalence rate of diabetes is rising quickly in recent years
The increase of logKa for these interactions is worth attention. These results indicate that the modifications of human serum albumin (HSA) induced by glycation might affect the interactions between flavonoids and HSA at separate binding sites
It could be assumed that the affinity for glycated HSA enhanced with the increasing hydroxy groups in flavonoids and the hydrogen bonding might play a crucial part in the interaction between glycated HSA and flavonoids
Summary
Diabetes, which is known as diabetes mellitus, has become a big challenge in human health all over the world, and the prevalence rate of diabetes is rising quickly in recent years. As reported by the references, about twenty to thrity percent of human serum albumin (HSA) in the body of diabetes patients was glycated. As active compounds widely distributed in foods, dietary flavonoids have shown inhibitory effects on formation of AGEs [10,11,12]. They are identified as inhibitors of many human digestive enzymes, which makes them drug candidates for diabetes mellitus [13]. Fluorescence spectroscopy is a typical and appropriate method to investigate the interaction between small molecules like dietary flavonoids and biological macromolecules [17]. All other reagents and solvents were analytical grade and used without further purification
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