Graphene Symmetry Amplified by Designed Peptide Self-Assembly.
Graphene Symmetry Amplified by Designed Peptide Self-Assembly.
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DOI：
10.1016/j.bpj.2016.04.037
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发表时间：
2016-06-07
影响因子：
3.4
通讯作者：
Wanunu M
中科院分区：
文献类型：
--
作者：
Mustata GM;Kim YH;Zhang J;DeGrado WF;Grigoryan G;Wanunu M
我们提出了一种策略，设计的自组装成二维单层晶体的石墨烯和石墨表面的肽。正如计算所预测的那样，设计的肽在石墨烯表面组装，形成非常长的，平行的，对齐的β-片层，我们称之为β-带。肽垂直于每个β带的长轴延伸，限定其宽度，氢键沿着轴沿着延伸。胶带在表面上对齐，以创建包含4 nm间距条纹的高度规则的微区。此外，与计算结果一致，底层石墨烯的原子结构决定了β带的排列，因为它们沿着石墨烯的六重对称性所定义的六个方向之沿着。这里显示阳离子组装的肽表面强烈地粘附于DNA，优先使双螺旋沿着β-带轴定向。考虑到潜在的肽层结构，从计算中可以很好地预测这种取向偏好。这些研究说明了设计的肽如何将表面的朗格斯特伦水平原子对称性放大到微米尺度，进一步赋予下一级组装的长程方向有序性。这些组件在各种环境条件下的显着稳定的性质表明在酶催化，细胞识别的生物界面，和研究DNA-肽相互作用的二维平台中的应用。
We present a strategy for designed self-assembly of peptides into two-dimensional monolayer crystals on the surface of graphene and graphite. As predicted by computation, designed peptides assemble on the surface of graphene to form very long, parallel, in-register β-sheets, which we call β-tapes. Peptides extend perpendicularly to the long axis of each β-tape, defining its width, with hydrogen bonds running along the axis. Tapes align on the surface to create highly regular microdomains containing 4-nm pitch striations. Moreover, in agreement with calculations, the atomic structure of the underlying graphene dictates the arrangement of the β-tapes, as they orient along one of six directions defined by graphene’s sixfold symmetry. A cationic-assembled peptide surface is shown here to strongly adhere to DNA, preferentially orienting the double helix along β-tape axes. This orientational preference is well anticipated from calculations, given the underlying peptide layer structure. These studies illustrate how designed peptides can amplify the Ångstrom-level atomic symmetry of a surface onto the micrometer scale, further imparting long-range directional order onto the next level of assembly. The remarkably stable nature of these assemblies under various environmental conditions suggests applications in enzymelike catalysis, biological interfaces for cellular recognition, and two-dimensional platforms for studying DNA-peptide interactions.