Molecular simulation study of peptide amphiphile self-assembly
Molecular simulation study of peptide amphiphile self-assembly
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DOI：
10.1021/jp074420n
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发表时间：
2008-02-28
影响因子：
3.3
通讯作者：
de la Cruz, Monica Olvera
中科院分区：
文献类型：
--
作者：
Velichko, Yuri S.;Stupp, Samuel I.;de la Cruz, Monica Olvera
我们研究了肽两亲（PA）分子的自组装，这是由烷基尾部之间的疏水相互作用和肽块之间的氢键网络所控制的。我们证明了这两种相互作用之间的相互作用导致了不同形态的组件的形成，特别是通过氢键横向连接的单个p片，平行p片的堆叠，球形胶束，日冕中p片的胶束和长圆柱形纤维。我们将聚集体的大小分布描述为分子相互作用的函数。我们的研究结果表明，肽类两亲体纳米纤维的聚合遵循一个开放的缔合模式，类似于活聚合。
We study the self-assembly of peptide amphiphile (PA) molecules, which is governed by hydrophobic interactions between alkyl tails and a network of hydrogen bonds between peptide blocks. We demonstrate that the interplay between these two interactions results in the formation of assemblies of different morphology, in particular, single P-sheets connected laterally by hydrogen bonds, stacks of parallel P-sheets, spherical micelles, micelles with P-sheets in the corona, and long cylindrical fibers. We characterize the size distribution of the aggregates as a function of the molecular interactions. Our results suggest that the fort-nation of nanofibers of peptide amphiphiles obeys an open association model, which resembles living polymerization.