光谱法研究甲苯达唑与牛血清白蛋白的相互作用  

Investigation of Binding Interactions Between Mebendazole with Bovine Serum Albumin by Multispectroscopy

作　　者：顾佳丽[1] 王思宇 杨丹 黄曦瑶 何茜 秦洪伟[1] GU Jiali;WANG Siyu;YANG Dan;HUANG Xiyao;HE Qian;QIN Hongwei(College of Chemistry and Chemical Engineering,Bohai University,Jinzhou 121013)

机构地区：[1]渤海大学化学化工学院,辽宁锦州121013

出　　处：《分析科学学报》2020年第6期857-862,共6页Journal of Analytical Science

基　　金：国家自然科学基金(No.41602351)。

摘　　要：本文采用多种光谱法研究了甲苯达唑(MBZ)与牛血清白蛋白(BSA)之间的相互作用机制。荧光猝灭实验及时间分辨荧光实验结果表明:MBZ对BSA的荧光猝灭主要为静态猝灭;温度298 K时二者的结合常数与结合位点数分别为6.52×10^4 L·mol^-1和1.08;热力学参数ΔH与ΔS分别为-117.49 kJ·mol^-1和-229.24 J·mol^-1·K^-1,说明MBZ与BSA之间的作用力主要为范德华力和氢键。位点竞争实验结果表明MBZ结合在BSA亚结构域ⅡA的SiteⅠ。紫外-可见光谱、同步荧光光谱、红外光谱法以及圆二色光谱实验结果表明,MBZ诱导BSA的构象发生变化。Mebendazole(MBZ) is veterinary drug commonly used for antiparasitic control in domestic animal,but its residues in edible animals products may pose potential toxic to human health.The binding mechanism between MBZ and bovine serum albumin(BSA) was investigated by multispectroscopy.The results of fluorescence quenching and time-resolved fluorescence measurements showed that quenching of BSA by MBZ was mainly static quenching.The binding constants and number of binding sites were 6.52×10^4 L·mol^-1 and 1.08 at 298 K,respectively.The thermodynamic parameters enthalpy and entropy were-117.49 kJ·mol^-1 and-229.24 J·mol^-1·K^-1,indicating that the interaction between BSA and MBZ were van der waals forces and hydrogen bond.The results of site marker competitive experiments suggested that MBZ could bound BSA into site Ⅰ in subdomain ⅡA.The conformation of BSA was changed after the interaction with MBZ,which were verified by the results of UV-Vis spectroscopy,synchronous fluorescence spectroscopy,fourier transform infrared spectroscopy and circular dichroism spectroscopy.

关 键 词：甲苯达唑 牛血清白蛋白 相互作用 

分 类 号：O657.3[理学—分析化学]