Characterizing the binding interaction of fungicide boscalid with bovine serum albumin (BSA): A spectroscopic study in combination with molecular docking approach
Characterizing the binding interaction of fungicide boscalid with bovine serum albumin (BSA): A spectroscopic study in combination with molecular docking approach
复制标题
DOI：
10.1016/j.jphotobiol.2017.06.037
复制
发表时间：
2017-08-01
影响因子：
5.4
通讯作者：
Pan, Dong-Qi
中科院分区：
文献类型：
--
作者：
Lou, Yan-Yue;Zhou, Kai-Li;Pan, Dong-Qi
啶酰菌胺是一种酰胺类杀菌剂，用于防治灰霉病和白粉病，广泛应用于水稻、小麦、葡萄、梨等多种作物和水果。由于其广泛的应用和在农作物和水果中的残留，将成为潜在的健康风险。本研究采用稳态荧光光谱、紫外光谱、同步荧光光谱、三维荧光光谱、傅立叶变换红外光谱和分子对接等方法，研究啶酰菌胺与牛血清白蛋白（BSA）的结合作用，探讨啶酰菌胺在牛血清白蛋白体内的储存、转运和分布。实验结果表明，在298 K下，啶酰菌胺与BSA形成静态复合物，结合常数为4.57 × 10（3）M-1，并通过货车德瓦尔斯力和氢键作用与BSA的Ⅲ A亚结构域（位点Ⅱ）结合，从而使BSA的荧光猝灭。在所研究的温度范围内，啶酰菌胺与BSA的结合过程是自发的，基于Delta G（0）< 0 and vertical bar Delta H-0 vertical bar >T垂直棒Delta S-0垂直棒的双稳态驱动过程。同时，啶酰菌胺与牛血清白蛋白结合后，其构象发生了明显的变化，而牛血清白蛋白的构象发生了轻微的变化，这表明啶酰菌胺的柔性有助于提高复合物的稳定性。
Boscalid, a carboxamide fungicide, is used in the treatment of grey mould and powdery mildew, widely applied to a variety of crops and fruits such as rice, wheat, grapes and pears. It will become a potential risk for health due to its widely application and residue in crops and fruits. In this study, the binding interaction between boscalid and bovine serum albumin (BSA) was characterized using steady-state fluorescence spectroscopy, ultraviolet spectroscopy (UV), synchronous fluorescence spectroscopy, 3D fluorescence spectroscopy, Fourier transform infrared spectroscopy (FT-IR) and molecular docking to ascertain the store, transport and distribution of boscalid in vivo. The experimental results indicated that the fluorescence of BSA was quenched due to the forming the static boscalid-BSA complex with the binding constant of 4.57 x 10(3) M-1 at 298 K and boscalid bound on the subdomain III A (site II) of BSA through van der Waals force and hydrogen bonding interaction. The binding process of boscalid with BSA was spontaneous and enthalpy-driven process based on Delta G(0) < 0 and vertical bar Delta H-0 vertical bar > T vertical bar Delta S-0 vertical bar over the studied temperature range. Meanwhile, the obvious change in the conformation of boscalid was observed while the slight change in the conformation of BSA when binding boscalid to the BSA, implying that the flexibility of boscalid contributes to increasing the stability of the boscalid-BSA complex.