牛血清白蛋白与双子表面活性剂链烷二基-α,ω-双(二甲基十二烷基溴化铵)之间的相互作用。
Interactions between bovine serum albumin and gemini surfactant alkanediyl-alpha, omega-bis(dimethyldodecyl-ammonium bromide).
作者信息
Pi Yingying, Shang Yazhuo, Peng Changjun, Liu Honglai, Hu Ying, Jiang Jianwen
机构信息
Department of Chemistry and Lab for Advanced Materials, East China University of Science and Technology, Shanghai 200237, China.
出版信息
Biopolymers. 2006 Oct 15;83(3):243-9. doi: 10.1002/bip.20552.
Interactions between bovine serum albumin (BSA) and cationic gemini surfactant alkanediyl-alpha,omega-bis(dimethyldodecyl-ammonium bromide) (12-n-12, n=3, 4, 6) in aqueous solution have been investigated by measuring fluorescence, UV-vis transmittance, dynamic lighting scattering, and circular dichroism. Compared to a traditional surfactant dodecyltrimethylammonium bromide (DTAB), 12-n-12 interacts with BSA more strongly. With increasing concentration, 12-n-12 first binds specifically onto BSA leading to the unfolding and aggregation of BSA, and the decrease in alpha-helix content; and then forms micelle-like complexes along the unfolded BSA chains. A gemini surfactant with a longer spacer has a larger effect on BSA unfolding due to a stronger hydrophobic interaction.
通过测量荧光、紫外可见透光率、动态光散射和圆二色性，研究了水溶液中牛血清白蛋白（BSA）与阳离子双子表面活性剂链烷二基-α,ω-双（二甲基十二烷基溴化铵）（12-n-12，n = 3、4、6）之间的相互作用。与传统表面活性剂十二烷基三甲基溴化铵（DTAB）相比，12-n-12与BSA的相互作用更强。随着浓度的增加，12-n-12首先特异性地结合到BSA上，导致BSA的展开和聚集，以及α-螺旋含量的降低；然后沿着展开的BSA链形成类似胶束的复合物。由于更强的疏水相互作用，具有较长间隔基的双子表面活性剂对BSA展开的影响更大。
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