title: Probing into the binding interaction between medroxyprogesterone acetate and bovine serum albumin (BSA): spectroscopic and molecular docking methods.
abstract: To further understand the mechanism of action and pharmacokinetics of medroxyprogesterone acetate (MPA), the binding interaction of MPA with bovine serum albumin (BSA) under simulated physiological conditions (pH 7.4) was studied using fluorescence emission spectroscopy, synchronous fluorescence spectroscopy, circular dichroism and molecular docking methods. The experimental results reveal that the fluorescence of BSA quenches due to the formation of MPA-BSA complex. The number of binding sites (n) and the binding constant for MPA-BSA complex are ~1 and 4.6 × 10(3)  M(-1) at 310 K, respectively. However, it can be concluded that the binding process of MPA with BSA is spontaneous and the main interaction forces between MPA and BSA are van der Waals force and hydrogen bonding interaction due to the negative values of ΔG(0) , ΔH(0) and ΔS(0) in the binding process of MPA with BSA. MPA prefers binding on the hydrophobic cavity in subdomain IIIA (site II'') of BSA resulting in a slight change in the conformation of BSA, but BSA retaining the α-helix structure. Copyright © 2016 John Wiley & Sons, Ltd.
authors.affiliation: College of Pharmaceutical Science, Zhejiang University of Technology, Hangzhou, 310032, China.
authors.forename: Fang
authors.initials: F
authors.lastname: Fang
authors.affiliation: College of Pharmaceutical Science, Zhejiang University of Technology, Hangzhou, 310032, China.
authors.forename: Dong-Qi
authors.initials: DQ
authors.lastname: Pan
authors.affiliation: College of Pharmaceutical Science, Zhejiang University of Technology, Hangzhou, 310032, China.
authors.forename: Min-Jie
authors.initials: MJ
authors.lastname: Qiu
authors.affiliation: College of Pharmaceutical Science, Zhejiang University of Technology, Hangzhou, 310032, China.
authors.forename: Ting-Ting
authors.initials: TT
authors.lastname: Liu
authors.affiliation: College of Pharmaceutical Science, Zhejiang University of Technology, Hangzhou, 310032, China.
authors.forename: Min
authors.initials: M
authors.lastname: Jiang
authors.affiliation: College of Pharmaceutical Science, Zhejiang University of Technology, Hangzhou, 310032, China.
authors.forename: Qi
authors.initials: Q
authors.lastname: Wang
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.
authors.forename: Jie-Hua
authors.initials: JH
authors.lastname: Shi
mesh_terms: D000818:Animals; D001665:Binding Sites; D002417:Cattle; D002942:Circular Dichroism; D017258:Medroxyprogesterone Acetate / Q000737:chemistry*; D062105:Molecular Docking Simulation; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013050:Spectrometry, Fluorescence
chemical_list: D012710:Serum Albumin, Bovine; D017258:Medroxyprogesterone Acetate
keywords: bovine serum albumin; interaction; medroxyprogesterone acetate; molecular docking; spectroscopy