Interaction between bovine serum albumin and equimolarly mixed cationic-anionic surfactants decyltriethylammonium bromide-sodium decyl sulfonate
Interaction between bovine serum albumin and equimolarly mixed cationic-anionic surfactants decyltriethylammonium bromide-sodium decyl sulfonate
复制标题
DOI：
10.1016/j.colsurfb.2004.11.011
复制
发表时间：
2005-03-25
影响因子：
5.8
通讯作者：
Xiao, JX
中科院分区：
文献类型：
--
作者：
Lu, RC;Cao, AN;Xiao, JX
通过表面张力、粘度、动态光散射(DLS)和圆环法研究了牛血清白蛋白(BSA)与阴离子表面活性剂癸基磺酸钠(C10SO3)、阳离子表面活性剂癸基三乙基溴化铵(C10NE)以及等摩尔混合的阴阳离子表面活性剂C10NE-C10SO3的相互作用。 二色性（M）。结果表明，单一离子表面活性剂C10SO3或C10NE与BSA有明显的相互作用。 C10SO3或C10NE的存在修饰了BSA结构。然而，等摩尔混合的阳离子-阴离子表面活性剂C10NE-C10SO3与BSA的相互作用非常弱。 C10NE-C10SO3/BSA 混合物水溶液的表面张力对数浓度 (gamma-log C) 图与 C10NE-C10SO3 溶液的表面张力对数浓度图一致。粘度测定表明C10NE-C10SO3/BSA混合溶液的流变性质没有显着变化。 DLS表明C10NE-C10SO3/BSA混合溶液中存在BSA单体和C10NE-C10SO3混合聚集体。从 CD 光谱来看，在 C10NE-C10SO3 混合物存在下，没有观察到 BSA 结构的明显改变。 BSA 和 C10NE-C10SO3 之间的弱相互作用可能是因为 C10NE-C10SO3 混合物的临界胶束浓度 (cmc) 非常低，这使得离子表面活性剂单体的浓度远低于诱导 BSA 结构修饰所需的浓度。换句话说，带相反电荷的阳离子和阴离子表面活性剂之间的非常强的协同作用使得在本体溶液中形成阳离子-阴离子表面活性剂混合聚集体是比与蛋白质结合更有利的过程。 (c) 2004 Elsevier B.V. 保留所有权利。
The interactions of bovine serum albumin (BSA) with the anionic surfactant sodium decylsulfonate (C10SO3), the cationic surfactant decyltriethylammonium bromide (C10NE) and equimolarly mixed cationic-anionic surfactants C10NE-C10SO3 were investigated by surface tension, viscosity, dynamic light scattering (DLS) and circular dichroism (M). It was shown that the single ionic surfactant C10SO3 or C10NE has obvious interaction with BSA. The presence Of C10SO3 or C10NE modified BSA structure. However, the equimolarly mixed cationic-anionic surfactants C10NE-C10SO3 Showed very weak interactions with BSA. The surface tension-log concentration (gamma-log C) plot for the aqueous solutions of C10NE-C10SO3/BSA mixtures coincided with that of C10NE-C10SO3 solutions. Viscometry showed that there is no significant change in the rheological properties for the C10NE-C10SO3/BSA mixed solutions. DLS showed that BSA monomers and mixed aggregates of C10NE-C10SO3 existed in the C10NE-C10SO3/BSA mixed solutions. From CD spectra no obvious modification of BSA structure in the presence of C10NE-C10SO3 Mixtures was observed. The weak interactions between BSA and C10NE-C10SO3 might be explained in terms of the very low critical micelle concentration (cmc) of C10NE-C10SO3 mixtures that made the concentration of ionic surfactant monomers much lower than that needed for inducing the modification of BSA structure. In other words, the very strong synergism between oppositely charged cationic and anionic surfactants makes the formation of cationic-anionic surfactant mixed aggregates in the bulk solution a more favorable process than binding to proteins. (c) 2004 Elsevier B.V. All rights reserved.