Glycation of human serum albumin alters its binding efficacy towards the dietary polyphenols: a comparative approach. Issue 9 (1st September 2016)

• Record Type: Journal Article
• Authors: Singha Roy, Atanu; Ghosh, Pooja; Dasgupta, Swagata
• Is Part Of: Journal of biomolecular structure & dynamics. Volume 34:Issue 9(2016)
• Page Start: 1911
• Page End: 1918
• Publication Date: 2016-09-01
• Subjects: glycation -- human serum albumin -- dietary polyphenols -- binding constant -- fluorescence spectroscopy; Biomolecules -- Periodicals; Molecular structure -- Periodicals; Molecular Biology -- Periodicals; Biomechanics -- Periodicals; 572
• DOI: 10.1080/07391102.2015.1094749
• Languages: English
• ISSNs: 0739-1102

Abstract

Abstract : Diabetes is a major problem in the world. The proteins became modified during glycation after reacting with the reducing sugars (e.g. D-glucose) via non-enzymatic pathways. The glycated analogue of human serum albumin (HSA) has been characterized with the help of multi-spectroscopic methods. It has been observed that six glucose molecules can bind covalently to HSA under experimental condition. The binding affinity of the modified HSA towards the dietary polyphenols has been estimated using UV–vis and fluorescence spectroscopic techniques. The binding constant values of the ligands were found to decrease after the modification of HSA. Graphical abstract: The binding affinities ( K b ) of the polyphenols decreased towards human serum albumin after its structural modification with D-glucose. Highest percentage decrease in the binding is observed for quercetin among all the polyphenols.