Department of Chemistry, University of Kashmir, Srinagar, J&K, India.
Colloids Surf B Biointerfaces. 2010 May 1;77(1):54-9. doi: 10.1016/j.colsurfb.2010.01.005. Epub 2010 Jan 14.
The interactions of bovine serum albumin (BSA) with cationic gemini surfactants alkanediyl-alpha,omega-bis(dimethylcetylammonium bromide) (designated as C(16)C(s)C(16)Br(2), s=4, 5, and 6) and single chain surfactant cetyltrimethylammonium bromide (CTAB) have been investigated with tensiometry, Rayleigh's scattering, fluorescence spectroscopy, and circular dichroism at physiological pH and 25 degrees C. The results of the multi-technique approach showed that the gemini surfactants interact more efficiently with the proteins than their conventional single chain counterparts and their efficiency increases with decrease in the length of the spacer. The saturation in interfacial tension occurred at a lower concentration in presence of BSA compared to CMC of the surfactants in absence of BSA and the concentration of gemini surfactants corresponding to interfacial saturation decreases with decrease in the spacer length. Fluorescence and circular dichroism spectroscopy results revealed increase in unfolding of BSA with decrease in spacer length of gemini surfactants.
牛血清白蛋白（BSA）与阳离子双子表面活性剂烷二基-α，ω-双（二甲基十六烷基溴化铵）（指定为 C(16)C(s)C(16)Br(2)，s=4、5 和 6）和单链表面活性剂十六烷基三甲基溴化铵（CTAB）在生理 pH 值和 25°C 下通过张力计、瑞利散射、荧光光谱和圆二色性进行了相互作用研究。多技术方法的结果表明，双子表面活性剂与蛋白质的相互作用比其常规的单链对应物更有效，并且其效率随间隔物长度的减小而增加。与不存在 BSA 的表面活性剂的 CMC 相比，在存在 BSA 时，界面张力的饱和度在较低浓度下发生，并且对应于界面饱和的双子表面活性剂的浓度随间隔物长度的减小而降低。荧光和圆二色性光谱结果表明，随着双子表面活性剂间隔物长度的减小，BSA 的展开增加。
