Srivastava Rachana, Alam Md Sayem
Council of Scientific and Industrial Research (CSIR) - Central Leather Research Institute (CLRI), Polymer Science &Technology Laboratory, Chennai 600020, India.
Council of Scientific and Industrial Research (CSIR) - Central Leather Research Institute (CLRI), Polymer Science &Technology Laboratory, Chennai 600020, India; Chemical Science, Academy of Scientific and Innovative Research (AcSIR), Ghaziabad, Uttar Pradesh- 201 002, India.
Int J Biol Macromol. 2020 May 4;158:394-400. doi: 10.1016/j.ijbiomac.2020.04.254.
To check the role of micelle in the interaction studies of human serum albumin (HSA) and cetyltrimethylammonium bromide (CTAB), many spectroscopic techniques, like UV-visible, fluorescence, circular dichroism, fluorescence lifetime measurement, and atomic force microscopy (AFM), are employed. The binding affinity of all compound groups depended on the hydrocarbon chain, indicating the predominant role of hydrophobic forces, electrostatic forces and supported by polar interactions on protein surfaces. The protein has a different effect on the polarity of a microenvironment in fluorescence spectra above and below the critical micelle concentration (CMC) of the suractant. The far-UV-CD spectra show unfolding below the CMC and refolding above the CMC. The binding of the surfactant induces changes in the microenvironment at different pHs around the residues of the aromatic amino acid and the disulfide bond of protein. The AFM images show significant changes in the protein's structure. AFM images show dense aggregation below the CMC and above the CMC, some net-like structure formed in the HSA-CTAB complex. To test the experimental results, we used Auto dock Vina to conduct molecular docking. Above and below the CMC, structural changes can be seen.
为了研究胶束在人血清白蛋白（HSA）与十六烷基三甲基溴化铵（CTAB）相互作用研究中的作用，采用了多种光谱技术，如紫外可见光谱、荧光光谱、圆二色光谱、荧光寿命测量和原子力显微镜（AFM）。所有化合物组的结合亲和力都取决于烃链，表明疏水作用力、静电力起主要作用，并得到蛋白质表面极性相互作用的支持。在表面活性剂的临界胶束浓度（CMC）以上和以下的荧光光谱中，蛋白质对微环境的极性有不同的影响。远紫外圆二色光谱显示在CMC以下蛋白质展开，在CMC以上蛋白质重新折叠。表面活性剂的结合会导致蛋白质芳香族氨基酸残基和二硫键周围不同pH值下微环境的变化。AFM图像显示蛋白质结构有显著变化。AFM图像显示在CMC以下和以上有密集聚集，在HSA-CTAB复合物中形成了一些网状结构。为了验证实验结果，我们使用Auto dock Vina进行分子对接。在CMC以上和以下都可以看到结构变化。
