罗非昔布与牛血清白蛋白之间相互作用的研究  

Study on the Interaction Between Rofecoxib and Bovine Serum Albumin

作　　者：刘昭清 万众 江政 庹浔 LIU Zhaoqing;WAN Zhong;JIANG Zheng;TUO Xun(College of Chemistry,Nanchang University,Nanchang 330000;School of Pharmacy,Nanchang University,Nanchang 330000)

机构地区：[1]南昌大学化学学院,江西南昌330000 [2]南昌大学药学院,江西南昌330000

出　　处：《分析科学学报》2020年第3期421-426,共6页Journal of Analytical Science

基　　金：国家自然科学基金(No.31860153);江西省自然科学基金(No.20181BAB204003)。

摘　　要：在模拟人体生理条件下,通过荧光光谱法、紫外光谱法、红外光谱法和分子对接等技术探究罗非昔布(RFB)与牛血清白蛋白(BSA)之间相互作用的化学本质。研究结果表明,RFB与BSA的Trp/Tyr残基之间的π-π堆积作用诱导了BSA的荧光发生猝灭,其猝灭机制为静态猝灭并且伴随着非辐射能量的转移;热力学参数表明RFB-BSA可以自发地通过氢键与范德华力进行结合,二者之间的结合距离r 0=3.50 nm,且结合位点数为1;同步荧光和分子对接结果证明RFB与BSA在结合位点Ⅰ结合;三维荧光光谱与红外光谱揭示了RFB导致BSA蛋白质二级结构发生变化,其中α-螺旋和β-片层结构含量下降,β-折叠和β-转角含量上升。In simulative physiological environment(pH=7.4), the interactions between rofecoxib(RFB) and bovine serum albumin(BSA) were investigated by spectroscopic and molecular docking techniques. The results revealed that the mechanism of fluorescence quenching was a static quenching and non-radiative energy transfer. According to the Vant’s Hoff equation, the thermodynamic parameters were calculated to be ΔS=-268.21 J/(mol·K), ΔH=-109.5 kJ/mol, indicating that the predominant forces in the complex were hydrogen bonding and Van der Waals forces. The result of synchronous fluorescence and molecular docking results indicated that RFB bound to the site I of BSA. The three-dimensional fluorescence spectrum and FT-IR spectroscopy demonstrated that the micro-environment of BSA changed in the BSA-RFB complexes.

关 键 词：罗非昔布 牛血清白蛋白 光谱学 分子对接 相互作用 

分 类 号：O657.39[理学—分析化学]