Intermolecular forces in the self-assembly of peptide amphiphile nanofibers
Intermolecular forces in the self-assembly of peptide amphiphile nanofibers
复制标题
DOI：
10.1002/adfm.200500161
复制
发表时间：
2006-03-03
影响因子：
19
通讯作者：
Stupp, SI
中科院分区：
文献类型：
--
作者：
Stendahl, JC;Rao, MS;Stupp, SI
肽两亲分子（PAs）在我们的实验室开发的自组装从水介质成三维网络的生物活性纳米纤维。多重非共价相互作用促进超分子纳米纤维的组装，并最终决定宏观凝胶的本体物理性质。在这项研究中，我们使用振荡流变学，傅里叶变换红外光谱，和圆二色性光谱，以更好地了解一个典型的PA分子的组装机制称为PA-1的PA-1的自组装是由反屏蔽触发和稳定的货车德瓦尔斯和疏水力，离子桥，配位和氢键。浓度，电子结构。反离子的水合作用显著影响自组装和凝胶力学性能。
Peptide amphiphile molecules (PAs) developed in our laboratory self-assemble from aqueous media into three-dimensional networks of bioactive nanofibers. Multiple non-covalent interactions promote assembly of the supramolecular nanofibers and ultimately determine the bulk physical properties of the macroscopic gels. In this Study, we use oscillatory rheology, Fourier-transform infrared spectroscopy, and circular-dichroism spectroscopy to better understand the assembly mechanism of a typical PA molecule known as PA-1 Self-assembly of PA-1 is triggered by counterion screening and stabilized by van der Waals and hydrophobic forces, ionic bridging, and coordination and hydrogen bonding. The concentration, electronic structure. and hydration of counterions significantly influence self-assembly and gel mechanical properties.