Protein Structure and Dynamics in Ionic Liquids. Insights from Molecular Dynamics Simulation Studies

分子动力学 动力学(音乐) 离子液体 化学物理 蛋白质动力学 离子键合 统计物理学 化学 计算机科学 计算化学 物理 离子 生物化学 有机化学 声学 催化作用
作者
Nuno M. Micaêlo,Cláudio M. Soares
出处
期刊:Journal of Physical Chemistry B [American Chemical Society]
卷期号:112 (9): 2566-2572 被引量:199
标识
DOI:10.1021/jp0766050
摘要

We present in this work the first molecular simulation study of an enzyme, the serine protease cutinase from Fusarium solani pisi, in two ionic liquids (ILs): 1-butyl-3-methylimidazolium hexafluorophosphate ([BMIM][PF6]) and 1-butyl-3-methylimidazolium nitrate ([BMIM][NO3]). We tested different water contents in these ILs at room temperature (298 K) and high temperature (343 K), and we observe that the enzyme structure is highly dependent on the amount of water present in the IL media. We show that the enzyme is preferentially stabilized in [BMIM][PF6] at 5−10% (w/w) (weight of water over protein) water content at room temperature. [BMIM][PF6] renders a more nativelike enzyme structure at the same water content of 5−10% (w/w) as previously found for hexane, and the system displays a similar bell-shape-like dependence with the water content in the IL media. [BMIM][PF6] is shown to increase significantly the protein thermostability at high temperatures, especially at low hydration. Our analysis indicates that the enzyme is less stabilized in [BMIM][NO3] relative to [BMIM][PF6] at both temperatures, most likely due to the strong affinity of the [NO3]- anion toward the protein main chain. These findings are in accordance with the experimental knowledge for these two ionic liquids. We also show that these ILs "strip off" most of the water from the enzyme surface in a degree similar to that found for polar organic solvents such as acetonitrile, and that the remaining waters at the enzyme surface are organized in many small clusters.
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