Two-dimensional honeycomb network through sequence-controlled self-assembly of oligopeptides.
Two-dimensional honeycomb network through sequence-controlled self-assembly of oligopeptides.
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DOI：
10.1038/ncomms10335
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发表时间：
2016-01-12
影响因子：
16.6
通讯作者：
Kern K
中科院分区：
文献类型：
--
作者：
Abb S;Harnau L;Gutzler R;Rauschenbach S;Kern K
肽的序列编程了它的自组装，从而通过非共价相互作用表达了特定的性质。利用这些非共价相互作用的不同方面，如色散相互作用、氢键或离子相互作用，已经设计出了种类繁多的肽纳米结构。在这里，我们展示了利用肽作为二维（2D）自组装的生物有机构建块的分子纳米结构的序列控制制造。扫描隧道显微镜揭示了通过序列修饰去除位阻的结果，从紧凑或线性组合（血管紧张素I）到远程有序的手性蜂窝网络（血管紧张素II）的变化。在我们观察的指导下，分子动力学模拟产生了解释肽间结合基序的原子模型。这种在表面上进行二维自组装的新方法提供了在原子水平上的洞察力，这将使使用寡聚肽和多肽作为大的、多功能的生物有机构建块成为可能，并为合理设计的、受生物启发的表面开辟了新的途径。肽纳米结构由于其在医学、电子和涂料方面的潜在应用而引起了人们的兴趣。在这里，通过实验和理论，作者展示了通过操纵氨基酸序列对表面肽组装行为的精细控制。
The sequence of a peptide programs its self-assembly and hence the expression of specific properties through non-covalent interactions. A large variety of peptide nanostructures has been designed employing different aspects of these non-covalent interactions, such as dispersive interactions, hydrogen bonding or ionic interactions. Here we demonstrate the sequence-controlled fabrication of molecular nanostructures using peptides as bio-organic building blocks for two-dimensional (2D) self-assembly. Scanning tunnelling microscopy reveals changes from compact or linear assemblies (angiotensin I) to long-range ordered, chiral honeycomb networks (angiotensin II) as a result of removal of steric hindrance by sequence modification. Guided by our observations, molecular dynamic simulations yield atomistic models for the elucidation of interpeptide-binding motifs. This new approach to 2D self-assembly on surfaces grants insight at the atomic level that will enable the use of oligo- and polypeptides as large, multi-functional bio-organic building blocks, and opens a new route towards rationally designed, bio-inspired surfaces. Peptide nanostructures are currently arousing interest thanks to their potential applications in medicine, electronics and coatings. Here, through experiment and theory, the authors demonstrate exquisite control over surface peptide assembly behaviour through manipulation of amino acid sequence.