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首页> 外文期刊>Journal of Biomolecular Structure and Dynamics >Molecular dynamics simulations of adrenocorticotropin (1-24) peptide in a solvated dodecylphosphocholine (DPC) micelle and in a dimyistoylphosphatidylcholine (DMPC) bilayer.
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Molecular dynamics simulations of adrenocorticotropin (1-24) peptide in a solvated dodecylphosphocholine (DPC) micelle and in a dimyistoylphosphatidylcholine (DMPC) bilayer.

机译：溶剂化的十二烷基磷脂酰胆碱（DPC）胶束和二甲苯基磷脂酰胆碱（DMPC）双层中肾上腺皮质激素（1-24）肽的分子动力学模拟。

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摘要

The structure and interactions of the 1-24 fragment of the adrenocorticotropin hormone, ACTH (1-24), with membrane have been studied by molecular dynamics (MD) simulation in an NPT ensembles in two explicit membrane mimics, a dodecylphosphocholine (DPC) micelle and a dimyristoylphosphatidylcholine (DMPC) bilayer. The starting configuration of the peptide/lipid systems had the 1-10 segment of the peptide lying on the surface of the model membrane, the same as the equilibrated structure (by MD) of ACTH (1-10) in a DPC micelle. The simulations showed that the peptide adopts the surface-binding mode and essentially the same structure in both systems. Thus the results of this work lend support to the assumption that micelles are reasonable mimics for biological membranes for the study of peptide binding. The 1-10 segment is slightly tilted from the parallel orientation to the interface and interacts strongly with the membrane surface while the more polar 11-24 segment shows little tendency to interact with the membrane surface, preferring to reside primarily in the aqueous phase. Furthermore, the 1-10 segment of the peptide binds to the DPC micelle in essentially the same way as ACTH (1-10). Thus the MD results are in excellent agreement with the model of interaction of ACTH (1-24) with membrane derived from NMR experiments. The secondary structure and the hydration of the peptide and the interactions of specific residues with the lipid head groups have also been analyzed.
机译：肾上腺皮质激素激素ACTH（1-24）的1-24片段与膜的结构和相互作用已通过分子动力学（MD）模拟在两个明确的膜模拟物（十二烷基磷酸胆碱（DPC）胶束）中的NPT集成中进行了研究和二豆蔻酰磷脂酰胆碱（DMPC）双层。肽/脂质系统的起始构型具有位于模型膜表面的肽的1-10片段，与DPC胶束中ACTH（1-10）的平衡结构（按MD）相同。模拟表明，该肽在两个系统中均采用表面结合模式且结构基本相同。因此，这项工作的结果支持以下假设：胶束是用于研究生物膜的肽结合的合理模拟物。 1-10链段从平行方向稍微倾斜到界面，并与膜表面发生强烈相互作用，而极性更大的11-24链段则几乎没有与膜表面发生相互作用的趋势，而是主要位于水相中。此外，该肽的1-10区段以与ACTH（1-10）基本上相同的方式与DPC胶束结合。因此，MD结果与ACTH（1-24）与来自NMR实验的膜的相互作用模型非常吻合。还分析了肽的二级结构和水合以及特定残基与脂质头基的相互作用。

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