Membrane composition-mediated protein-protein interactions
Membrane composition-mediated protein-protein interactions
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DOI：
10.1116/1.2977492
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发表时间：
2008-06
期刊：
影响因子：
2.1
通讯作者：
B. Reynwar;M. Deserno
中科院分区：
文献类型：
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作者：
B. Reynwar;M. Deserno
作者研究了膜组成介导的蛋白质之间的相互作用吸附到一个双组分脂质双层接近临界分层使用粗粒度的分子动力学模拟和现象学的金斯堡-朗道理论。模拟由三珠脂质和板状蛋白，吸附到膜上的结合优先的两种脂质物种之一。一个蛋白质和两个蛋白质之间的对相关函数的组成分布进行测量，并与分析预测进行比较。该理论框架适用于任何标量场嵌入在膜，虽然在这项工作中，作者处理平面膜，该方法很容易扩展到弯曲的几何形状。忽略波动，脂质组成的配置文件和诱导蛋白质对潜在的预测遵循零阶修改的贝塞尔函数的第二类具有相同的特征衰减长度。这些预测与我们的分子动力学模拟是一致的，除了相互作用的范围被发现是大于单一配置文件的相关长度。
The authors investigate membrane composition-mediated interactions between proteins adsorbed onto a two-component lipid bilayer close to critical demixing using coarse-grained molecular dynamics simulations and a phenomenological Ginzburg-Landau theory. The simulations consist of three-bead lipids and platelike proteins, which adsorb onto the membrane by binding preferentially to one of the two lipid species. The composition profile around one protein and the pair correlation function between two proteins are measured and compared to the analytical predictions. The theoretical framework is applicable to any scalar field embedded in the membrane, and although in this work the authors treat flat membranes, the methodology extends readily to curved geometries. Neglecting fluctuations, both lipid composition profile and induced protein pair potential are predicted to follow a zeroth order modified Bessel function of the second kind with the same characteristic decay length. These predictions are consistent with our molecular dynamics simulations, except that the interaction range is found to be larger than the single profile correlation length.