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Graphene Symmetry Amplified by Designed Peptide Self-Assembly

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Title
Graphene Symmetry Amplified by Designed Peptide Self-Assembly
Author(s)
Gina-Mirela Mustata; Yong Ho Kim; Jian Zhang; William F. DeGrado; Gevorg Grigoryan; Meni Wanunu
Publication Date
2016-06
Journal
BIOPHYSICAL JOURNAL, v.110, no.11, pp.2507 - 2516
Publisher
CELL PRESS
Abstract
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. © 2016 Biophysical Society
URI
https://pr.ibs.re.kr/handle/8788114/2565
ISSN
0006-3495
Appears in Collections:
Center for Neuroscience Imaging Research (뇌과학 이미징 연구단) > Journal Papers (저널논문)
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