Structural Polymorphism in a Self-Assembled Tri-Aromatic Peptide System.
Structural Polymorphism in a Self-Assembled Tri-Aromatic Peptide System.
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DOI：
10.1021/acsnano.7b07723
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发表时间：
2018-04-24
期刊：
影响因子：
17.1
通讯作者：
Gazit E
中科院分区：
文献类型：
--
作者：
Brown N;Lei J;Zhan C;Shimon LJW;Adler-Abramovich L;Wei G;Gazit E
自组装在自然系统和纳米技术中是一个非常重要的过程。肽由于其相对容易的合成、生物相容性和其他独特的性质而成为有吸引力的结构单元。已知二苯丙氨酸（FF）及其衍生物形成各种结构和有趣且变化的特性的纳米结构。发现较大的三苯基丙氨酸肽（FFF）自组装效率与FF一样高，形成相关但不同的板状和球形纳米结构。在这里，为了了解三芳族系统的自组装过程中的效果，我们研究了羧苄基保护的二苯丙氨酸（z-FF）作为这样的安排的最小模型。我们探索了不同的自组装条件下，通过改变溶剂的组成和肽的浓度，生成的组件的相图。我们发现z-FF可以形成各种结构，包括纳米线、纤维、纳米球和纳米环，后者以前只在相当大的或共组装系统中观察到。二级结构分析表明，组装体均为β折叠构象。此外，在具有高水比率的溶剂组合中，z-FF形成刚性和自愈合水凝胶。X射线晶体学显示了“叉骨”结构，其中z-FF二聚体通过由甲醇分子介导的氢键连接，沿c轴沿着具有2重螺旋对称性。全原子分子动力学（MD）模拟显示构象类似的晶体结构。粗粒分子动力学模拟了在不同溶剂体系中肽组装成纤维或球体的过程，与实验结果一致。因此，这项工作扩大了构建模块库的肽自组装纳米结构的制造。
Self-assembly is a process of key importance in natural systems and in nanotechnology. Peptides are attractive building blocks due to their relative facile synthesis, biocompatibility, and other unique properties. Diphenylalanine (FF) and its derivatives are known to form nanostructures of various architectures and interesting and varied characteristics. The larger triphenylalanine peptide (FFF) was found to self-assemble as efficiently as FF, forming related but distinct architectures of plate-like and spherical nanostructures. Here, to understand the effect of triaromatic systems on the self-assembly process, we examined carboxybenzyl-protected diphenylalanine (z-FF) as a minimal model for such an arrangement. We explored different self-assembly conditions by changing solvent compositions and peptide concentrations, generating a phase diagram for the assemblies. We discovered that z-FF can form a variety of structures, including nanowires, fibers, nanospheres, and nanotoroids, the latter were previously observed only in considerably larger or co-assembly systems. Secondary structure analysis revealed that all assemblies possessed a β-sheet conformation. Additionally, in solvent combinations with high water ratios, z-FF formed rigid and self-healing hydrogels. X-ray crystallography revealed a “wishbone” structure, in which z-FF dimers are linked by hydrogen bonds mediated by methanol molecules, with a 2-fold screw symmetry along the c-axis. All-atom molecular dynamics (MD) simulations revealed conformations similar to the crystal structure. Coarse-grained MD simulated the assembly of the peptide into either fibers or spheres in different solvent systems, consistent with the experimental results. This work thus expands the building block library for the fabrication of nanostructures by peptide self-assembly.
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影响因子：
5.5
作者：
Caleman, Carl;van Maaren, Paul J.;Hong, Minyan;Hub, Jochen S.;Costa, Luciano T.;van der Spoel, David
通讯作者：
van der Spoel, David
影响因子：
5.5
作者：
Hess, Berk;Kutzner, Carsten;Lindahl, Erik
通讯作者：
Lindahl, Erik
影响因子：
2.9
作者：
HARIS, PI;CHAPMAN, D
通讯作者：
CHAPMAN, D
影响因子：
21.8
作者：
Frederix, Pim W. J. M.;Scott, Gary G.;Tuttle, Tell
通讯作者：
Tuttle, Tell
影响因子：
4
作者：
Bosne, E. D.;Heredia, A.;Kholkin, A. L.
通讯作者：
Kholkin, A. L.