Patgar Manjanath, Durgannavar Amar, Nandibewoor Sharanappa, Chimatadar Shivamurti
P. G. Department of Studies in Chemistry, Karnatak University, Pavate Nagar, Dharwad, 580003, Karnataka, India.
J Mol Recognit. 2017 Feb;30(2). doi: 10.1002/jmr.2567. Epub 2016 Oct 3.
The mechanism of the interaction between bovine serum albumin (BSA) and desvenlafaxine was studied using fluorescence, ultraviolet absorption, 3-dimensional fluorescence spectroscopy, circular dichroism, synchronous fluorescence spectroscopy, cyclic voltametry, differential scanning calorimetry, and attenuated total reflection-Fourier transform infrared spectroscopic techniques under physiological condition at pH 7.4. Stern-Volmer calculations authenticate the fluorescence of BSA that was quenched by desvenlafaxine in a collision quenching mode. The fluorescence quenching method was used to evaluate number of binding sites "n" and binding constant K that were measured, and various thermodynamic parameters were evaluated at different temperatures by using the van't Hoff equation and differential scanning calorimetry technique, which indicated a spontaneous and hydrophobic interaction between BSA and desvenlafaxine. According to the Förster theory we calculate the distance between the donor, BSA and acceptor, desvenlafaxine molecules. Furthermore, circular dichroism and attenuated total reflection-Fourier transform infrared spectroscopy indicate nominal changes in the secondary structure of the protein.
在pH 7.4的生理条件下，采用荧光、紫外吸收、三维荧光光谱、圆二色性、同步荧光光谱、循环伏安法、差示扫描量热法和衰减全反射-傅里叶变换红外光谱技术研究了牛血清白蛋白（BSA）与去甲文拉法辛之间的相互作用机制。斯特恩-沃尔默计算证实了去甲文拉法辛以碰撞猝灭模式猝灭了BSA的荧光。采用荧光猝灭法评估所测得的结合位点数量“n”和结合常数K，并通过范特霍夫方程和差示扫描量热法在不同温度下评估了各种热力学参数，结果表明BSA与去甲文拉法辛之间存在自发的疏水相互作用。根据福斯特理论，我们计算了供体BSA与受体去甲文拉法辛分子之间的距离。此外，圆二色性和衰减全反射-傅里叶变换红外光谱表明蛋白质二级结构有明显变化。
