Influence of glycation of plasma proteins in diabetes on the binding interaction with polyphenols

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 diet...

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Bibliographic Details
Published inCurrent drug metabolism Vol. 15; no. 1; p. 116
Main Authors Xu, Wei, Chen, Longsheng, Shao, Rong
Format Journal Article
LanguageEnglish
Published Netherlands 01.01.2014
Subjects
Diabetes Mellitus - metabolism
Glycosylation
Humans
Polyphenols - pharmacokinetics
Protein Binding
Serum Albumin - metabolism
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Summary: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.
ISSN:1875-5453
DOI:10.2174/1389200215666140130141823