Self-assembly of coherently dynamic, auxetic, two-dimensional protein crystals.
Self-assembly of coherently dynamic, auxetic, two-dimensional protein crystals.
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DOI:
10.1038/nature17633
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发表时间:
2016-05-19
期刊:
影响因子:
64.8
通讯作者:
Tezcan FA
中科院分区:
文献类型:
--
作者:
Suzuki Y;Cardone G;Restrepo D;Zavattieri PD;Baker TS;Tezcan FA
Two-dimensional (2D) crystalline materials possess unique structural, mechanical, and electronic properties, which have rendered them highly attractive in many applications. Although there have been advances in preparing 2D materials that consist of one or few atomic/molecular layers, bottom-up assembly of 2D crystalline materials remains a considerable challenge and an active area of development. Even more challenging is the design of dynamic 2D lattices that can undergo large-scale motions without loss of crystallinity. Dynamicity in porous 3D crystalline solids has been exploited for stimuli-responsive functions and adaptive behavior. As in the case of such 3D materials, integrating flexibility/adaptiveness into crystalline 2D lattices would greatly broaden the functional scope of 2D materials. Here we report the self-assembly of unsupported, 2D protein lattices with precise spatial arrangements and patterns through a readily accessible design strategy. Three single- or double-point mutants of the C4 symmetric protein RhuA were designed to assemble via different modes of intermolecular interactions (single disulfide, double disulfide and metal coordination) into crystalline 2D arrays. Owing to the flexibility of the single disulfide interactions, the lattices of one of the variants (C98RhuA) are essentially defect-free and undergo substantial but fully correlated changes in molecular arrangement, giving coherently dynamic 2D molecular lattices. Notably, C98RhuA lattices possess a Poisson's ratio of −1, the lowest thermodynamically possible value for an isotropic material.