title: Mechanism and conformational studies of farrerol binding to bovine serum albumin by spectroscopic methods.
abstract: The mechanism and conformational changes of farrerol binding to bovine serum albumin (BSA) were studied by spectroscopic methods including fluorescence quenching technique, UV-vis absorption, circular dichroism (CD) spectroscopy and Fourier transform infrared (FT-IR) spectroscopy under simulative physiological conditions. The results of fluorescence titration revealed that farrerol could strongly quench the intrinsic fluorescence of BSA through a static quenching procedure. The thermodynamic parameters enthalpy change and entropy change for the binding were calculated to be -29.92 kJ mol(-1) and 5.06 J mol(-1) K(-1) according to the van't Hoff equation, which suggested that the both hydrophobic interactions and hydrogen bonds play major role in the binding of farrerol to BSA. The binding distance r deduced from the efficiency of energy transfer was 3.11 nm for farrerol-BSA system. The displacement experiments of site markers and the results of fluorescence anisotropy showed that warfarin and farrerol shared a common binding site I corresponding to the subdomain IIA of BSA. Furthermore, the studies of synchronous fluorescence, CD and FT-IR spectroscopy showed that the binding of farrerol to BSA induced conformational changes in BSA.
authors.affiliation: State Key Laboratory of Food Science and Technology, Nanchang University, 235, Nanjing East Road, Nanchang 330047, Jiangxi, China. gwzhang@ncu.edu.cn
authors.forename: Guowen
authors.initials: G
authors.lastname: Zhang
authors.forename: Lin
authors.initials: L
authors.lastname: Wang
authors.forename: Peng
authors.initials: P
authors.lastname: Fu
authors.forename: Mingming
authors.initials: M
authors.lastname: Hu
mesh_terms: D000818:Animals; D000975:Antioxidants / Q000737:chemistry; D002417:Cattle; D002867:Chromones / Q000737:chemistry*; D002942:Circular Dichroism / Q000379:methods; D008956:Models, Chemical; D008968:Molecular Conformation; D011485:Protein Binding; D011487:Protein Conformation; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013050:Spectrometry, Fluorescence / Q000379:methods; D013053:Spectrophotometry / Q000379:methods*; D017550:Spectroscopy, Fourier Transform Infrared / Q000379:methods; D013816:Thermodynamics
chemical_list: D000975:Antioxidants; D002867:Chromones; C015881:farrerol; D012710:Serum Albumin, Bovine