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首页> 外文期刊>Biochemistry >Molecular Dynamics Simulations of Pentapeptides at Interfaces: Salt Bridge and Cation-pi Interactions.
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Molecular Dynamics Simulations of Pentapeptides at Interfaces: Salt Bridge and Cation-pi Interactions.

机译：五肽在界面上的分子动力学模拟：盐桥和阳离子-π相互作用。

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Peptide-membrane interactions are important for understanding the binding, partitioning, and folding of membrane proteins; the activity of antimicrobial and fusion peptides; and a number of other processes. We describe molecular dynamics simulations (10-25 ns) of two pentapeptides Ace-WLXLL (with X = Arg or Lys side chain) (White, S. H., and Wimley, W.C. (1996) Nat. Struct. Biol. 3, 842-848) in water and three different membrane mimetic systems: (i) a water/cyclohexane interface, (ii) water-saturated octanol, and (iii) a solvated dioleoylphosphatidylcholine bilayer. A salt bridge is found between the protonated Arg or Lys side chains with the carboxyl terminus at the three interfaces. In water/cyclohexane, the salt bridge is most exposed to the water phase and least stable. In water/octanol and the lipid bilayer systems, the salt bridge once formed persists throughout the simulations. In the lipid bilayer, the salt bridge is more stable when the peptide penetrates deeper into the bilayer. In one of twopeptides, a cation-pi interaction between the Arg and the Trp side chains is stable in the lipid bilayer for about 15 ns before breaking. In all cases, the conformations of the peptides are restricted by their presence at the interface and can be assigned to a few major conformational clusters. Side chains facing the water phase are most mobile. In the lipid bilayer, the peptides remain in the interface area, where they overlap with the carbonyl area of the lipid bilayer and perturb the local density profile of the bilayer. The tryptophan side chain remains in the water-lipid interface, where it interacts with the lipid choline group and forms hydrogen bonds with the ester carbonyl of the lipid and with water in the interface.
机译：肽-膜相互作用对于理解膜蛋白的结合，分配和折叠很重要。抗菌肽和融合肽的活性;以及许多其他过程。我们描述了两个五肽Ace-WLXLL（X = Arg或Lys侧链）的分子动力学模拟（10-25 ns）（White，SH和Wimley，WC（1996）Nat。Struct。Biol。3，842-848） ）在水和三种不同的膜模拟系统中：（i）水/环己烷界面，（ii）水饱和的辛醇，和（iii）溶剂化的二油酰基磷脂酰胆碱双层。在质子化的Arg或Lys侧链与三个界面处的羧基末端之间发现了一个盐桥。在水/环己烷中，盐桥最容易暴露于水相中，并且不稳定。在水/辛醇和脂质双层系统中，一旦形成的盐桥将在整个模拟过程中持续存在。在脂质双层中，当肽更深地渗入双层时，盐桥更稳定。在两个肽之一中，Arg和Trp侧链之间的阳离子-π相互作用在脂双层中稳定约15 ns，然后才断裂。在所有情况下，肽的构象都受到其在界面处的存在的限制，并且可以分配给一些主要的构象簇。面向水相的侧链最易移动。在脂质双层中，肽保留在界面区域中，在此处与脂质双层的羰基区域重叠并扰乱了双层的局部密度分布。色氨酸侧链保留在水-脂质界面中，在此处它与脂质胆碱基团相互作用，并与脂质的酯羰基和界面中的水形成氢键。

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