title: Studies on the interaction between benzophenone and bovine serum albumin by spectroscopic methods.
abstract: The interaction between benzophenone (BP) and bovine serum albumin (BSA) was investigated by the methods of fluorescence spectroscopy combined with UV-Vis absorption and circular dichroism (CD) measurements under simulative physiological conditions. The experiment results showed that the fluorescence quenching of BSA by BP was resulted from the formation of a BP-BSA complex and the corresponding association constants (Ka) between BP and BSA at four different temperatures had been determined using the modified Stern-Volmer equation. The enthalpy change (ΔH) and entropy change (ΔS) were calculated to be -43.73 kJ mol(-1) and -53.05 J mol(-1) K(-1), respectively, which suggested that hydrogen bond and van der Waals force played major roles in stabilizing the BP-BSA complex. Site marker competitive experiments indicated that the binding of BP to BSA primarily took place in site I (sub-domain IIA). The conformational investigation showed that the presence of BP decreased the α-helical content of BSA and induced the slight unfolding of the polypeptides of protein, which confirmed some micro-environmental and conformational changes of BSA molecules.
authors.affiliation: Department of Chemistry, College of Chemistry and Environmental Engineering, Yangtze University, Jingzhou, 434023, Hubei, People's Republic of China. zhangfluorescence@126.com
authors.forename: Ye-Zhong
authors.initials: YZ
authors.lastname: Zhang
authors.forename: Jing
authors.initials: J
authors.lastname: Zhang
authors.forename: Fang-Fang
authors.initials: FF
authors.lastname: Li
authors.forename: Xun
authors.initials: X
authors.lastname: Xiang
authors.forename: A-Qiong
authors.initials: AQ
authors.lastname: Ren
authors.forename: Yi
authors.initials: Y
authors.lastname: Liu
mesh_terms: D000818:Animals; D001577:Benzophenones / Q000378:metabolism*; D002417:Cattle; D002942:Circular Dichroism; D019277:Entropy; D006860:Hydrogen Bonding; D015394:Molecular Structure; D011485:Protein Binding; D011487:Protein Conformation; D012710:Serum Albumin, Bovine / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D013696:Temperature; D013816:Thermodynamics
chemical_list: D001577:Benzophenones; D012710:Serum Albumin, Bovine; C047723:benzophenone