摘要
蛋白质分子和界面之间的作用在药物输送以及生物分离等领域至关重要。利用分子动力学模拟考察蛋白质分子在界面附近的行为是最近10年研究的热点。在早期的工作中,Wang等发现同电荷离子交换介质可用于辅助蛋白质复性,但其机理不甚明确。在利用分子动力学模拟研究其分子机理时发现,不同静电作用力参数对模拟结果有直接的影响。因此,通过全原子分子动力学模拟考察不同静电参数条件对模拟结果的影响,展示此过程的构象和能量变化,分析了造成结果差异的原因。研究结果揭示了不同静电参数对模拟结果的影响,为进一步研究蛋白质在界面表面的行为奠定了一定的理论基础。
The study of interactions between protein molecules and interfaces are essential for a number of applications such as drug delivery and biotechnical separation. The interactions between proteins and interfaces have been studied frequently by molecular dynamics （MD） simulations in the last ten years. In the early work, it is confirmed that the like-charged ion-exchange resin is efficient to suppress the aggregation of the protein folding intermediates, leading to a significant increase of native protein recovery by Wang. However, the working mechanism was not clarified. It was found the chosen of electrostatic interaction functions were significant on the results of the MD simulations. In the present study, the role of the electrostatic interaction functions in the all-atom MD simulations was studied; the conformation and the energy change in the process were calculated to reveal the reasons of the difference results. These results provide molecular insights into the effect of electrostatic interaction functions on the molecular dynamics simulations results. Furthermore, a theoretical foundation was established for the further research on the interactions between proteins and interfaces.
出处
《化学工业与工程》
CAS
2014年第5期74-79,共6页
Chemical Industry and Engineering
关键词
静电作用力算法
带电表面
分子动力学模拟
分子机理
electrostatic interaction functions
charged surface
molecular dynamics simulations
molecular mechanism
