Probing into the binding interaction between medroxyprogesterone acetate and bovine serum albumin (BSA): spectroscopic and molecular docking methods

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• 作者：Fang Fang ; Dong-qi Pan ; Min-jie Qiu ; Ting-Ting Liu ; Min Jiang ; Qi Wang and Jie-hua Shi
• 刊名：Luminescence
• 出版年：2016
• 出版时间：September 2016
• 年：2016
• 卷：31
• 期：6
• 页码：1242-1250
• 全文大小：1447K
• ISSN：1522-7243

文摘

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 × 10³ 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 ΔG⁰, ΔH⁰ and ΔS⁰ 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