Resveratrol, genistein, and curcumin bind bovine serum albumin

dc.contributor.author	Bourassa, P	en
dc.contributor.author	Kanakis, CD	en
dc.contributor.author	Tarantilis, P	en
dc.contributor.author	Pollissiou, MG	en
dc.contributor.author	Tajmir-Riahi, HA	en
dc.date.accessioned	2014-06-06T06:50:41Z
dc.date.available	2014-06-06T06:50:41Z
dc.date.issued	2010	en
dc.identifier.issn	15206106	en
dc.identifier.uri	http://dx.doi.org/10.1021/jp9115996	en
dc.identifier.uri	http://62.217.125.90/xmlui/handle/123456789/5117
dc.subject.other	Binding constant	en
dc.subject.other	Bovine serum albumins	en
dc.subject.other	Curcumin	en
dc.subject.other	FTIR	en
dc.subject.other	Genistein	en
dc.subject.other	Hydrophilic and hydrophobic interactions	en
dc.subject.other	Ligand binding mode	en
dc.subject.other	Physiological condition	en
dc.subject.other	Polyphenol content	en
dc.subject.other	Polyphenols	en
dc.subject.other	Protein concentrations	en
dc.subject.other	Protein unfolding	en
dc.subject.other	Resveratrol	en
dc.subject.other	Spectroscopic method	en
dc.subject.other	Turn structure	en
dc.subject.other	Binding energy	en
dc.subject.other	Complexation	en
dc.subject.other	Fourier transform infrared spectroscopy	en
dc.subject.other	Hydrophobicity	en
dc.subject.other	Phenols	en
dc.subject.other	Proteins	en
dc.subject.other	Spectroscopic analysis	en
dc.subject.other	Structural analysis	en
dc.subject.other	Body fluids	en
dc.subject.other	bovine serum albumin	en
dc.subject.other	curcumin	en
dc.subject.other	genistein	en
dc.subject.other	resveratrol	en
dc.subject.other	stilbene derivative	en
dc.subject.other	animal	en
dc.subject.other	article	en
dc.subject.other	cattle	en
dc.subject.other	chemistry	en
dc.subject.other	circular dichroism	en
dc.subject.other	hydrophobicity	en
dc.subject.other	infrared spectroscopy	en
dc.subject.other	protein binding	en
dc.subject.other	protein denaturation	en
dc.subject.other	protein secondary structure	en
dc.subject.other	spectrofluorometry	en
dc.subject.other	Animals	en
dc.subject.other	Cattle	en
dc.subject.other	Circular Dichroism	en
dc.subject.other	Curcumin	en
dc.subject.other	Genistein	en
dc.subject.other	Hydrophobicity	en
dc.subject.other	Protein Binding	en
dc.subject.other	Protein Denaturation	en
dc.subject.other	Protein Structure, Secondary	en
dc.subject.other	Serum Albumin, Bovine	en
dc.subject.other	Spectrometry, Fluorescence	en
dc.subject.other	Spectroscopy, Fourier Transform Infrared	en
dc.subject.other	Stilbenes	en
dc.title	Resveratrol, genistein, and curcumin bind bovine serum albumin	en
heal.type	journalArticle	en
heal.identifier.primary	10.1021/jp9115996	en
heal.publicationDate	2010	en
heal.abstract	We report the complexation of bovine serum albumin (BSA) with resveratrol, genistein, and curcumin, at physiological conditions, using constant protein concentration and various polyphenol contents. FTIR, CD, and fluorescence spectroscopic methods were used to analyze the ligand binding mode, the binding constant, and the effects of complexation on BSA stability and conformation. Structural analysis showed that polyphenols bind BSA via hydrophilic and hydrophobic interactions with the number of bound polyphenol (n) being 1.30 for resveratrol - BSA, 1.30 for genisten - BSA, and 1.0 for curcumin - BSA. The polyphenol - BSA binding constants were KRes-BSA = 2.52(±0.5) × 104 M-1, KGen-BSA = 1.26(±0.3) × 104 M-1, and KCur-BSA = 3.33(=0.8) × 104 M-1. Polyphenol binding altered BSA conformation with a major reduction of a-helix and an increase in β-sheet and turn structures, indicating a partial protein unfolding. © 2010 American Chemical Society.	en
heal.journalName	Journal of Physical Chemistry B	en
dc.identifier.issue	9	en
dc.identifier.volume	114	en
dc.identifier.doi	10.1021/jp9115996	en
dc.identifier.spage	3348	en
dc.identifier.epage	3354	en