期刊
LANGMUIR
卷 30, 期 5, 页码 1343-1350出版社
AMER CHEMICAL SOC
DOI: 10.1021/la4043364
关键词
-
资金
- Lawrence Livermore National Laboratory [B601600]
- National Science Foundation [CMMI-0846858]
- Office of Science, Office of Basic Energy Sciences of the U.S. Department of Energy [DE-AC02-05CH11231, DE-AC52-07NA27344]
- Div Of Civil, Mechanical, & Manufact Inn
- Directorate For Engineering [0846858] Funding Source: National Science Foundation
Fibrillar collagens, common tissue scaffolds in live organisms, can also self-assemble in vitro from solution. While previous in vitro studies showed that the pH and the electrolyte concentration in solution largely control the collagen assembly, the physical reasons why such control could be exerted are still elusive. To address this issue and to be able to simulate self-assembly over large spatial and temporal scales, we have developed a microscopic model of collagen with explicit interactions between the units that make up the collagen molecules, as well as between these units and the substrate. We have used this model to investigate assemblies obtained via molecular dynamics deposition of collagen on a substrate at room temperature using an implicit solvent. By comparing the morphologies from our molecular dynamics simulations with those from our atomic-force microscopy experiments, we have found that the assembly is governed by the competition between the collagen-collagen interactions and those between collagen and the substrate. The microscopic model developed here can serve for guiding future experiments that would explore new regions of the parameter space.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据