Diabetes mellitus is one of the most serious diseases in the world. The degree of glycated plasma proteins is increased in diabetics
compared to non-diabetic subjects. This mini-review focuses on the influence of glycation of human serum albumin (HSA) in diabetes
on the binding interaction with dietary polyphenols. The non-enzymatic glycation of HSA leads to a conformational change in
HSA, which in turn influences the ligand binding properties. HSA glycation is believed to reduce the binding affinities for acidic drugs
such as dietary polyphenols and phenolic acids.
Keywords: Diabetes, glycation, human serum albumin, polyphenols, protein binding.
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