title: Glycation of human serum albumin alters its binding efficacy towards the dietary polyphenols: a comparative approach.
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.
authors.affiliation: a Department of Chemistry , Indian Institute of Technology , Kharagpur 721302 , India.
authors.forename: Atanu
authors.initials: A
authors.lastname: Singha Roy
authors.affiliation: a Department of Chemistry , Indian Institute of Technology , Kharagpur 721302 , India.
authors.forename: Pooja
authors.initials: P
authors.lastname: Ghosh
authors.affiliation: a Department of Chemistry , Indian Institute of Technology , Kharagpur 721302 , India.
authors.forename: Swagata
authors.initials: S
authors.lastname: Dasgupta
mesh_terms: D006031:Glycosylation; D006801:Humans; D015394:Molecular Structure; D059808:Polyphenols / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D012709:Serum Albumin / Q000737:chemistry* / Q000378:metabolism; D013050:Spectrometry, Fluorescence
chemical_list: D059808:Polyphenols; D012709:Serum Albumin
keywords: binding constant; dietary polyphenols; fluorescence spectroscopy; glycation; human serum albumin