New reverse micelle surfactant systems optimized for high-resolution NMR spectroscopy of encapsulated proteins.
New reverse micelle surfactant systems optimized for high-resolution NMR spectroscopy of encapsulated proteins.
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DOI：
10.1021/la051409a
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发表时间：
2005-09
期刊：
影响因子：
--
通讯作者：
Zhengshuang Shi;R. W. Peterson;A. Wand
中科院分区：
文献类型：
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作者：
Zhengshuang Shi;R. W. Peterson;A. Wand
双(2-乙基己基)琥珀酸磺酸钠(AOT)是一种表面活性剂，通常用于将水溶性蛋白质包裹在反胶束的水核中。在对被包裹的蛋白质进行高分辨率核磁共振研究的背景下，所产生的反胶束的大小至关重要。我们设计并合成了一种短的AOT类似物--3，3-二甲基-1-丁基磺基琥珀酸钠盐，并测定了它能够形成反胶束，并以较高的结构保真度包裹了蛋白质泛素。AOT经常被发现显著地破坏被包裹的蛋白质的稳定性，主要是通过阴离子头基和蛋白质表面之间的电荷相互作用。在这里，我们第一次证明，阴离子和阳离子表面活性剂的比例混合物可以形成反胶束，也能够高保真地包裹蛋白质。
Sodium bis(2-ethylhexyl)sulfosuccinate (AOT) is a surfactant commonly used to encapsulate water soluble proteins within the aqueous core of a reverse micelle. In the context of high-resolution NMR studies of encapsulated proteins the size of the resulting reverse micelle is critically important. We have designed and synthesized a short AOT analogue, 3,3-dimethyl-1-butylsulfosuccinate sodium salt and determined that it is able to form reverse micelles and to encapsulate the protein ubiquitin with high structural fidelity. AOT is often found to significantly destabilize encapsulated proteins, largely through charge-charge interactions between the anionic headgroup and the surface of the protein. Here we demonstrate, for the first time, that proportional mixtures of anionic and cationic surfactants can form reverse micelles that are also capable of protein encapsulation with high fidelity.