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Probing into the binding interaction between medroxyprogesterone acetate and bovine serum albumin (BSA): spectroscopic and molecular docking methods
Author(s) -
Fang Fang,
Pan Dongqi,
Qiu Minjie,
Liu TingTing,
Jiang Min,
Wang Qi,
Shi Jiehua
Publication year - 2016
Publication title -
luminescence
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.428
H-Index - 45
eISSN - 1522-7243
pISSN - 1522-7235
DOI - 10.1002/bio.3097
Subject(s) - bovine serum albumin , chemistry , circular dichroism , hydrogen bond , van der waals force , binding constant , binding site , fluorescence spectroscopy , hydrophobic effect , fluorescence , crystallography , chromatography , molecule , organic chemistry , biochemistry , physics , quantum mechanics
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 Δ G 0 , Δ H 0 and Δ S 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.