New reverse micelle surfactant systems optimized for high-resolution NMR spectroscopy of encapsulated proteins |
| |
Authors: | Shi Zhengshuang Peterson Ronald W Wand A Joshua |
| |
Institution: | Johnson Research Foundation and Department of Biochemistry & Biophysics, University of Pennsylvania, Philadelphia, 19104-6059, USA. |
| |
Abstract: | 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. |
| |
Keywords: | |
本文献已被 PubMed 等数据库收录! |
|