Glycine molecules in ionic liquid based reverse micelles: Investigation of structure and dynamics using molecular dynamics simulations
Glycine molecules in ionic liquid based reverse micelles: Investigation of structure and dynamics using molecular dynamics simulations
复制标题
DOI：
10.1016/j.molliq.2017.01.034
复制
发表时间：
2017-03
影响因子：
6
通讯作者：
S. Palchowdhury;B. L. Bhargava
中科院分区：
文献类型：
--
作者：
S. Palchowdhury;B. L. Bhargava
氨基酸是蛋白质的组成部分，在生物分子的反胶束包封过程中被探测。为了实现一个理论图片上的限制氨基酸的反胶束水核心的结构和动力学的影响，水/[C1 C10 Im][Br]反胶束含有可变数量的甘氨酸分子（0至8），分散在纯壬烷已使用原子分子动力学模拟研究。发现随着甘氨酸分子数目的增加，中心水池的大小变得稳定。甘氨酸分子通过氢键相互作用在反胶束的水性核心内缔合在一起。从反胶束水核心的质量中心的甘氨酸分子的径向密度分布示出了甘氨酸分子的中心附近的优先存在。与本体水溶液相比，纳米空间区域中的限制稳定了甘氨酸分子之间形成的氢键。反胶束水核内甘氨酸分子数量的增加了甘氨酸分子之间以及水分子之间H-键的存活时间。甘氨酸和水分子的平移和重定向运动被发现是直接相关的分子间甘氨酸-甘氨酸和水-水氢键的生存概率，这表明分子的流动性与氢键网络的重排之间的相关性。
Amino acids, the building blocks of proteins, are probed in reverse micellar encapsulation processes of biological molecules. To achieve a theoretical picture of the effect of confinement of amino acids on the structure and dynamics of reverse micellar aqueous core, a water/[C1C10Im][Br] reverse micelles containing variable number of glycine molecules (0 to 8), dispersed in pure nonane has been studied using atomistic molecular dynamics simulations. The size of the central water pool was found to become stable with increase in the number of glycine molecules. Glycine molecules associate together through H-bonding interaction within the aqueous core of the reverse micelles. The radial density profile of glycine molecules from the center of mass of the reverse micellar aqueous core shows the preferential presence of glycine molecules near the center. Confinement in nano-space region stabilizes the H-bonds formed between glycine molecules compared to bulk aqueous solution. Increase in the number of glycine molecules within the reverse micellar aqueous core increases the survival time of H-bonds among glycine molecules as well as among water molecules. Translational and reorientational motion of glycine and water molecules are found to be directly related to the survival probability of intermolecular glycine–glycine and water–water H-bonds suggesting the correlation between the mobility of molecules with the rearrangement of the H-bonding network.