Damodaran K V, Merz K M, Gaber B P
Department of Chemistry, Pennsylvania State University, University Park 16802, USA.
Biophys J. 1995 Oct;69(4):1299-308. doi: 10.1016/S0006-3495(95)79997-0.
Molecular dynamics simulations of the tripeptide Ala-Phe-Ala-O-tert-butyl interacting with dimyristoylphosphatidylcholine lipid bilayers have been carried out. The lipid and aqueous environments of the peptide, the alkyl chain order, and the lipid and peptide dynamics have been investigated with use of density profiles, radial distribution functions, alkyl chain order parameter profiles, and time correlation functions. It appears that the alkyl chain region accommodates the peptides in the bilayer with minimal perturbation to this region. The peptide dynamics in the bilayer bound form has been compared with that of the free peptide in water. The peptide structure does not vary on the simulation time scale (of the order of hundreds of picoseconds) compared with the solution structure in which a random structure is observed.
已经对三肽丙氨酸-苯丙氨酸-丙氨酸-叔丁酯与二肉豆蔻酰磷脂酰胆碱脂质双层相互作用进行了分子动力学模拟。利用密度分布、径向分布函数、烷基链序参数分布和时间相关函数，研究了肽的脂质和水环境、烷基链有序性以及脂质和肽的动力学。似乎烷基链区域在对该区域扰动最小的情况下将肽容纳在双层中。将双层结合形式的肽动力学与水中游离肽的动力学进行了比较。与观察到随机结构的溶液结构相比，在模拟时间尺度（数百皮秒量级）上肽结构没有变化。
