PDF(Pubmed)
Abstract：
Understanding mechanics of spider silk holds immense importance due to its potential to drive innovation in the development of materials with exceptional mechanical characteristics suited for a wide range of applications. Coarse-grained (CG) molecular simulations plays a particularly valuable role in this endeavor, allowing for the efficient investigation of spider silk\'s mechanical properties. Our research is centered on the examination of spider silk, which comprises major ampullate silk protein (MaSp1). To achieve this, we developed a CG molecular dynamics model. Our investigation began with a focus on MaSp1 chains subjected to uniaxial tensile load, with comparisons made between the CG model results and all-atom simulations. Subsequently, we extended our simulations to encompass more extensive systems, including fully-ordered MaSp1 bundles undergoing uniaxial static stretching. Through comparison with existing literature, we assess how well the CG model reproduces the mechanical properties of spider silk in highly ordered structures. Furthermore, we explored a scenario where MaSp1 bundles were randomly positioned and stretched, providing valuable insights into silk behavior when the initial structure lacks order. Another simulation involved random positioning, but with some degree of orientation in the loading direction, allowing for a closer examination of the initial structure\'s influence.
摘要：
了解蜘蛛丝的力学具有巨大的重要性，因为它有可能推动材料开发创新，具有适用于广泛应用的特殊机械特性。粗粒度(CG)分子模拟在这一努力中起着特别有价值的作用，允许有效研究蜘蛛丝的机械性能。我们的研究集中在蜘蛛丝的检查上，其包含主要的壶腹丝蛋白(MaSp1)。为了实现这一点，我们建立了CG分子动力学模型。我们的研究开始于MaSp1链受到单轴拉伸载荷，并将CG模型结果与全原子模拟进行了比较。随后，我们扩展了我们的模拟以涵盖更广泛的系统，包括进行单轴静态拉伸的完全有序的MaSp1束。通过与现有文献的比较，我们评估CG模型在高度有序结构中再现蜘蛛丝的机械性能的程度。此外，我们探索了一个场景，其中MaSp1束被随机定位和拉伸，当初始结构缺乏秩序时，为丝绸行为提供有价值的见解。另一个模拟涉及随机定位，但是在加载方向上有一定程度的定向，允许更仔细地检查初始结构的影响。
