Abstract
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.
Current Drug Metabolism
Title:Influence of Glycation of Plasma Proteins in Diabetes on the Binding Interaction with Polyphenols
Volume: 15 Issue: 1
Author(s): Wei Xu, Longsheng Chen and Rong Shao
Affiliation:
Keywords: Diabetes, glycation, human serum albumin, polyphenols, protein binding.
Abstract: 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.
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Cite this article as:
Xu Wei, Chen Longsheng and Shao Rong, Influence of Glycation of Plasma Proteins in Diabetes on the Binding Interaction with Polyphenols, Current Drug Metabolism 2014; 15 (1) . https://dx.doi.org/10.2174/1389200215666140130141823
DOI https://dx.doi.org/10.2174/1389200215666140130141823 |
Print ISSN 1389-2002 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5453 |
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