Department of Physical Chemistry I, Faculty of Chemistry and Biochemistry, Ruhr-University, D-44780 Bochum, Germany.
Phys Chem Chem Phys. 2010 Feb 28;12(8):1756-63. doi: 10.1039/b921037g. Epub 2010 Jan 6.
The objective of this study is to characterize the effect of ionic liquids (ILs) on the stability of proteins with regard to denaturation, protein aggregation and the formation of folding intermediates. Ribonuclease A was used as a model protein. A variety of ILs were tested. Detailed results are reported for choline dihydrogenphosphate, which enhances the thermal stability of the native state, and 1-ethyl-3-methylimidazolium dicyanamide, which acts as a strong denaturant. Varied factors include the intrinsic properties of the samples such as the IL concentration and the pH value as well as external factors such as incubation conditions. The time course of the deactivation processes was monitored. ILs can be used to suppress protein aggregation and steer the formation of intermediates.
本研究的目的是研究离子液体（ILs）对蛋白质变性、聚集和形成中间态稳定性的影响。使用核糖核酸酶 A 作为模型蛋白。测试了多种 ILs。详细结果报告了磷酸二氢胆碱，它增强了天然状态的热稳定性，以及 1-乙基-3-甲基咪唑二氰胺，它是一种强烈的变性剂。变化的因素包括样品的固有性质，如 IL 浓度和 pH 值以及外部因素，如孵育条件。监测了失活过程的时间过程。可以使用 ILs 来抑制蛋白质聚集并控制中间态的形成。
