title: Characterization of the interaction between eupatorin and bovine serum albumin by spectroscopic and molecular modeling methods.
abstract: This study investigated the interaction between eupatorin and bovine serum albumin (BSA) using ultraviolet-visible (UV-vis) absorption, fluorescence, synchronous fluorescence, circular dichroism (CD) spectroscopies, and molecular modeling at pH 7.4. Results of UV-vis and fluorescence spectroscopies illustrated that BSA fluorescence was quenched by eupatorin via a static quenching mechanism. Thermodynamic parameters revealed that hydrophobic and electrostatic interactions played major roles in the interaction. Moreover, the efficiency of energy transfer, and the distance between BSA and acceptor eupatorin, were calculated. The effects of eupatorin on the BSA conformation were analyzed using UV-vis, CD, and synchronous fluorescence. Finally, the binding of eupatorin to BSA was modeled using the molecular docking method.
authors.affiliation: Key Laboratory for Molecular Enzymology and Engineering of the Ministry of Education, College of Life Sciences, Jilin University, Changchun 130012, China. lzq@jlu.edu.cn.
authors.forename: Hongliang
authors.initials: H
authors.lastname: Xu
authors.forename: Nannan
authors.initials: N
authors.lastname: Yao
authors.forename: Haoran
authors.initials: H
authors.lastname: Xu
authors.forename: Tianshi
authors.initials: T
authors.lastname: Wang
authors.forename: Guiying
authors.initials: G
authors.lastname: Li
authors.forename: Zhengqiang
authors.initials: Z
authors.lastname: Li
mesh_terms: D000818:Animals; D002417:Cattle; D036602:Eupatorium / Q000737:chemistry*; D062105:Molecular Docking Simulation; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013057:Spectrum Analysis
chemical_list: D012710:Serum Albumin, Bovine