Self-assembly of β-sheet forming peptides into chiral fibrillar aggregates
Self-assembly of β-sheet forming peptides into chiral fibrillar aggregates
复制标题
DOI：
10.1063/1.2739547
复制
发表时间：
2007-06-28
影响因子：
4.4
通讯作者：
Shea, Joan-Emma
中科院分区：
文献类型：
--
作者：
Bellesia, Giovanni;Shea, Joan-Emma
作者介绍了一种新的中分辨率非晶格粗粒模型来研究β折叠形成肽的自组装。该模型保留了大部分肽骨架的自由度以及一个描述侧链的相互作用中心。肽由交替的疏水和亲水残基的核心组成，由两个带相反电荷的残基封端。非键相互作用用Lennard-Jones和Coulombic项描述。利用Langevin动力学研究了肽侧链之间不同水平的“疏水”力和“空间”力对聚集热力学和动力学的影响。该模型足够简单，可以模拟由数百种肽组成的系统，同时保持足够的现实性，成功地导致形成手性，有序的β带，带，以及更高阶的纤维状聚集体。(c)2007年，美国物理学会。
The authors introduce a novel mid-resolution off-lattice coarse-grained model to investigate the self-assembly of beta-sheet forming peptides. The model retains most of the peptide backbone degrees of freedom as well as one interaction center describing the side chains. The peptide consists of a core of alternating hydrophobic and hydrophilic residues, capped by two oppositely charged residues. Nonbonded interactions are described by Lennard-Jones and Coulombic terms. The influence of different levels of "hydrophobic" and "steric" forces between the side chains of the peptides on the thermodynamics and kinetics of aggregation was investigated using Langevin dynamics. The model is simple enough to allow the simulation of systems consisting of hundreds of peptides, while remaining realistic enough to successfully lead to the formation of chiral, ordered beta tapes, ribbons, as well as higher order fibrillar aggregates. (c) 2007 American Institute of Physics.