Simulations of a membrane-anchored peptide: Structure, dynamics, and influence on bilayer properties
Simulations of a membrane-anchored peptide: Structure, dynamics, and influence on bilayer properties
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DOI：
10.1529/biophysj.103.029140
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发表时间：
2004-06-01
影响因子：
3.4
通讯作者：
Peters, GH
中科院分区：
文献类型：
--
作者：
Jensen, MO;Mouritsen, OG;Peters, GH
一个模型十肽的三维结构是通过在显式水中进行肽的分子动力学模拟获得的。N-肉豆蔻酰化形式的折叠肽锚定二棕榈酰磷脂酰胆碱流体相脂质膜之间的相互作用进行了研究，在不同的应用表面张力的分子动力学模拟。脂质膜环境影响肽探索的构象空间。锚定肽的整体二级结构被发现偏离其在水溶液中的结构，通过可逆的构象转变的时间。尽管有锚，肽在膜表面是高度移动的，肽运动沿着双层法线被整合到膜的集体模式中。肽锚定通过改变膜的平衡面积适度地改变双层的侧向可压缩性。虽然膜锚定适度地影响双层的弹性性质，但是这里研究的模型肽表现出构象柔性，因此我们的结果表明肽酰化是一种可行的方式来加强肽-膜相互作用，可以延长受体-配体相互作用的寿命。
A three-dimensional structure of a model decapeptide is obtained by performing molecular dynamics simulations of the peptide in explicit water. Interactions between an N-myristoylated form of the folded peptide anchored to dipalmitoylphosphatidylcholine fluid phase lipid membranes are studied at different applied surface tensions by molecular dynamics simulations. The lipid membrane environment influences the conformational space explored by the peptide. The overall secondary structure of the anchored peptide is found to deviate at times from its structure in aqueous solution through reversible conformational transitions. The peptide is, despite the anchor, highly mobile at the membrane surface with the peptide motion along the bilayer normal being integrated into the collective modes of the membrane. Peptide anchoring moderately alters the lateral compressibility of the bilayer by changing the equilibrium area of the membrane. Although membrane anchoring moderately affects the elastic properties of the bilayer, the model peptide studied here exhibits conformational flexibility and our results therefore suggest that peptide acylation is a feasible way to reinforce peptide-membrane interactions whereby, e.g., the lifetime of receptor-ligand interactions can be prolonged.