title: Binding interaction of atorvastatin with bovine serum albumin: Spectroscopic methods and molecular docking.
abstract: The interaction of atorvastatin with bovine serum albumin (BSA) was investigated using multi-spectroscopic methods and molecular docking technique for providing important insight into further elucidating the store and transport process of atorvastatin in the body and the mechanism of action and pharmacokinetics. The experimental results revealed that the fluorescence quenching mechanism of BSA induced atorvastatin was a combined dynamic and static quenching. The binding constant and number of binding site of atorvastatin with BSA under simulated physiological conditions (pH=7.4) were 1.41 × 10(5) M(-1) and about 1 at 310K, respectively. The values of the enthalpic change (ΔH(0)), entropic change (ΔS(0)) and Gibbs free energy (ΔG(0)) in the binding process of atorvastatin with BSA at 310K were negative, suggesting that the binding process of atorvastatin and BSA was spontaneous and the main interaction forces were van der Waals force and hydrogen bonding interaction. Moreover, atorvastatin was bound into the subdomain IIA (site I) of BSA, resulting in a slight change of the conformation of BSA.
authors.affiliation: College of Pharmaceutical Sciences, Zhejiang University of Technology, Hangzhou 310032, China.
authors.forename: Qi
authors.initials: Q
authors.lastname: Wang
authors.affiliation: College of Pharmaceutical Sciences, Zhejiang University of Technology, Hangzhou 310032, China.
authors.forename: Chuan-ren
authors.initials: CR
authors.lastname: Huang
authors.affiliation: College of Pharmaceutical Sciences, Zhejiang University of Technology, Hangzhou 310032, China.
authors.forename: Min
authors.initials: M
authors.lastname: Jiang
authors.affiliation: College of Pharmaceutical Sciences, Zhejiang University of Technology, Hangzhou 310032, China.
authors.forename: Ying-yao
authors.initials: YY
authors.lastname: Zhu
authors.affiliation: College of Pharmaceutical Sciences, Zhejiang University of Technology, Hangzhou 310032, China.
authors.forename: Jing
authors.initials: J
authors.lastname: Wang
authors.affiliation: College of Pharmaceutical Sciences, Zhejiang University of Technology, Hangzhou 310032, China.
authors.forename: Jun
authors.initials: J
authors.lastname: Chen
authors.affiliation: College of Pharmaceutical Sciences, 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
mesh_terms: D000818:Animals; D000924:Anticholesteremic Agents / Q000737:chemistry / Q000378:metabolism*; D000069059:Atorvastatin / Q000737:chemistry / Q000378:metabolism*; D001665:Binding Sites; D002417:Cattle; D006860:Hydrogen Bonding; D062105:Molecular Docking Simulation; D011485:Protein Binding; D011487:Protein Conformation / Q000187:drug effects; D012710:Serum Albumin, Bovine / Q000737:chemistry / Q000378:metabolism*; D013816:Thermodynamics
chemical_list: D000924:Anticholesteremic Agents; D012710:Serum Albumin, Bovine; D000069059:Atorvastatin
keywords: Atorvastatin; Bovine serum albumin (BSA); Interaction; Molecular docking; Spectroscopy