Zhang Jie, Zhang Tiehua, Guan Tianzhu, Ruan Ping, Ren Dayong, Dai Weichang, Yu Hansong, Li Tiezhu
College of Food Science and Engineering, Jilin Agricultural University, Changchun 130118, China.
College of Food Science and Engineering, Jilin University, Changchun 130062, China.
Chemosphere. 2017 Aug;180:253-258. doi: 10.1016/j.chemosphere.2017.04.034. Epub 2017 Apr 9.
A fluorescence polarization (FP) assay for the simultaneous determination of bisphenol A (BPA), bisphenol F (BPF), bisphenol A diglycidyl ether (BADGE) and bisphenol F diglycidyl ether (BFDGE) was developed. The method was based on the competition between bisphenols (BPs) and fluorescein-labeled dexamethasone derivative (Dex-fl) for mouse peroxisome proliferator-activated receptor α ligand binding domain (mPPARα-LBD). A recombinant soluble protein derivative mPPARα-LBD* was prepared, then in vitro binding of 4 BPs to mPPARα-LBD* was investigated. Fluorescence polarization assay showed that these compounds exhibited different binding potencies with mPPARα-LBD*. Additionally, molecular dynamics simulations were performed to further understand the mechanism of BPs binding affinity for mPPARα-LBD*. Docking results elucidated that the driving forces for the binding of BPs to mPPARα-LBD* were predominantly dependent on hydrophobic and hydrogen-bonding interactions. Comparison of the calculated binding energies vs. experimental binding affinities yielded a good correlation (R = 0.7258). The proposed method has potential for multi-residue detection of BPA, BPF, BADGE, and BFDGE.
开发了一种用于同时测定双酚A（BPA）、双酚F（BPF）、双酚A二缩水甘油醚（BADGE）和双酚F二缩水甘油醚（BFDGE）的荧光偏振（FP）分析方法。该方法基于双酚类物质（BPs）与荧光素标记的地塞米松衍生物（Dex-fl）对小鼠过氧化物酶体增殖物激活受体α配体结合域（mPPARα-LBD）的竞争。制备了重组可溶性蛋白衍生物mPPARα-LBD*，然后研究了4种BPs与mPPARα-LBD的体外结合。荧光偏振分析表明，这些化合物与mPPARα-LBD表现出不同的结合能力。此外，进行了分子动力学模拟以进一步了解BPs对mPPARα-LBD的结合亲和力机制。对接结果表明，BPs与mPPARα-LBD结合的驱动力主要取决于疏水和氢键相互作用。计算得到的结合能与实验结合亲和力的比较产生了良好的相关性（R = 0.7258）。所提出的方法具有用于BPA、BPF、BADGE和BFDGE多残留检测的潜力。
