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 201002, India.
Spectrochim Acta A Mol Biomol Spectrosc. 2020 Oct 5;239:118542. doi: 10.1016/j.saa.2020.118542. Epub 2020 May 28.
The protein-surfactant interaction studies have great importance in the range of the application like cosmetics, food, pharmaceutical, detergent industries, and many more. In this study, we have studies protein (rabbit serum albumin, RSA) and a cationic surfactant (cetyltrimethylammonium bromide, CTAB) interaction at different physiological conditions (viz., pH, ionic strength, surfactants concentrations, protein concentration, and many more). They form the protein surfactant complexes. The interchange of electrostatic and hydrophobic force monitors the change in complexes. The three different pHs (below (4.0), above (7.0) and at (4.7) the isoelectric point of RSA) of the medium indicate the three different charges on the protein while surfactant is positive in charge. Critical micelle concentration (CMC) plays a significant role in protein-surfactant interaction. CTAB unfolds the protein at its specific concentration range afterward again; it starts refolded. RSA interacted, with the addition of the CTAB is characterized by many spectroscopic methods like UV-visible, fluorescence, fluorescence time-resolved, circular dichroism, and topographical changes monitored by the AFM. In fluorescence spectra, the blue shift shows the unfolding of RSA. The molecular docking indicates the binding energy of 5.8 kcal mol. The changes below and above the CMC is significant.
蛋白质 - 表面活性剂相互作用的研究在化妆品、食品、制药、洗涤剂等众多行业的应用领域具有重要意义。在本研究中，我们研究了蛋白质（兔血清白蛋白，RSA）与阳离子表面活性剂（十六烷基三甲基溴化铵，CTAB）在不同生理条件下（即pH值、离子强度、表面活性剂浓度、蛋白质浓度等）的相互作用。它们形成蛋白质 - 表面活性剂复合物。静电和疏水力的相互作用监测着复合物的变化。介质的三种不同pH值（低于（4.0）、高于（7.0）以及处于RSA的等电点（4.7））表明蛋白质上存在三种不同电荷，而表面活性剂带正电荷。临界胶束浓度（CMC）在蛋白质 - 表面活性剂相互作用中起着重要作用。CTAB在其特定浓度范围内会使蛋白质展开，之后又开始重新折叠。添加CTAB后RSA的相互作用通过多种光谱方法进行表征，如紫外可见光谱、荧光光谱、荧光时间分辨光谱、圆二色光谱以及通过原子力显微镜监测的形貌变化。在荧光光谱中，蓝移表明RSA发生了展开。分子对接表明结合能为5.8千卡/摩尔。CMC上下的变化是显著的。
