论文标题
Arg9（非A-精氨酸）和DOPC/DOPG（4：1）膜之间相互作用的分子动力学研究
Molecular dynamics studies of interactions between Arg9(nona-arginine) and a DOPC/DOPG(4:1) membrane
论文作者
论文摘要
众所周知，细胞穿透肽（CPP）的摄取机制取决于实验条件，例如肽的浓度，脂质成分，温度等。在这项研究中，我们研究了ARG9S中ARG9中的温度依赖性，使用分子动力学（4：1）使用分子动力学（MD）= 310 = 310 = 320 = 320由于在每个温度下只有一个单个模拟，并且在两个温度下都没有识别ARG9在整个膜中的易位的证据，因此难以识别温度依赖性，我们的模拟表明，跟随物与ARG9S的渗透密切相关：许多由ARG9S协调的水分子，Arg9s，Arg9s和Lipids Molecules之间的静电能。我们还介绍了ARG9如何改变膜的弯曲刚度以及ARG9之间的集体行为如何增强穿透性和膜弯曲。我们的分析可以适用于使用MD模拟的任何细胞渗透肽（CPP），以研究其与各种膜的相互作用。
It has been known that the uptake mechanisms of cell-penetrating peptides(CPPs) depend on the experimental conditions such as concentration of peptides, lipid composition, temperature, etc. In this study we investigate the temperature dependence of the penetration of Arg9s into a DOPC/DOPG(4:1) membrane using molecular dynamics(MD) simulations at two different temperatures, T = 310 K and T = 288 K. Although it is difficult to identify the temperature dependence because of having only one single simulation at each temperature and no evidence of translocation of Arg9s across the membrane at both temperatures, our simulations suggest that followings are strongly correlated with the penetration of Arg9s: a number of water molecules coordinated by Arg9s, electrostatic energy between Arg9s and the lipids molecules. We also present how Arg9s change a bending rigidity of the membrane and how a collective behavior between Arg9s enhances the penetration and the membrane bending. Our analyses can be applicable to any cell-penetrating peptides(CPPs) to investigate their interactions with various membranes using MD simulations.
