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Current Drug Metabolism

Editor-in-Chief

ISSN (Print): 1389-2002
ISSN (Online): 1875-5453

Influence of Glycation of Plasma Proteins in Diabetes on the Binding Interaction with Polyphenols

Author(s): Wei Xu, Longsheng Chen and Rong Shao

Volume 15, Issue 1, 2014

Page: [116 - 119] Pages: 4

DOI: 10.2174/1389200215666140130141823

Price: $65

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.


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