title: Binding interaction of sorafenib with bovine serum albumin: Spectroscopic methodologies and molecular docking.
abstract: The binding interaction of sorafenib with bovine serum albumin (BSA) was studied using fluorescence, circular dichrosim (CD) and molecular docking methods. The results revealed that there was a static quenching of BSA induced by sorafenib due to the formation of sorafenib-BSA complex. The binding constant and number of binding site of sorafenib with BSA under simulated physiological condition (pH=7.4) were 6.8×10(4) M(-1) and 1 at 310 K, respectively. Base on the sign and magnitude of the enthalpy and entropy changes (ΔH(0)=-72.2 kJ mol(-1) and ΔS(0)=-140.4J mol(-1) K(-1)) and the results of molecular docking, it could be suggested that the binding process of sorafenib and BSA was spontaneous and the main interaction forces of sorafenib with BSA were van der Waals force and hydrogen bonding interaction. From the results of site marker competitive experiments and molecular docking, it could be deduced that sorafenib was inserted into the subdomain IIA (site I) of BSA and leads to a slight change of the conformation of BSA. And, the significant change of conformation of sorafenib occurred in the binding process with BSA to increase the stability of the sorafenib-BSA system, implying that the flexibility of sorafenib played an important role in the binding process.
authors.affiliation: College of Pharmaceutical Science, Zhejiang University of Technology, Hangzhou 310032, China; State Key Laboratory Breeding Base of Green Chemistry Synthesis Technology, Zhejiang University of Technology, Hangzhou 310032, China. Electronic address: shijh@zjut.edu.cn.
authors.forename: Jie-Hua
authors.initials: JH
authors.lastname: Shi
authors.affiliation: College of Pharmaceutical Science, Zhejiang University of Technology, Hangzhou 310032, China.
authors.forename: Jun
authors.initials: J
authors.lastname: Chen
authors.affiliation: College of Pharmaceutical Science, Zhejiang University of Technology, Hangzhou 310032, China.
authors.forename: Jing
authors.initials: J
authors.lastname: Wang
authors.affiliation: College of Pharmaceutical Science, Zhejiang University of Technology, Hangzhou 310032, China.
authors.forename: Ying-Yao
authors.initials: YY
authors.lastname: Zhu
authors.affiliation: College of Pharmaceutical Science, Zhejiang University of Technology, Hangzhou 310032, China.
authors.forename: Qi
authors.initials: Q
authors.lastname: Wang
mesh_terms: D000818:Animals; D001665:Binding Sites; D002417:Cattle; D002942:Circular Dichroism; D004735:Energy Transfer; D007700:Kinetics; D062105:Molecular Docking Simulation; D009536:Niacinamide / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism; D010671:Phenylurea Compounds / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D012710:Serum Albumin, Bovine / Q000737:chemistry / Q000378:metabolism*; D000077157:Sorafenib; D013056:Spectrophotometry, Ultraviolet; D013816:Thermodynamics
chemical_list: D010671:Phenylurea Compounds; D009536:Niacinamide; D012710:Serum Albumin, Bovine; D000077157:Sorafenib
keywords: Bovine serum albumin; Circular dichroism; Fluorescence spectroscopy; Molecular docking; Sorafenib