期刊
ACS NANO
卷 12, 期 2, 页码 1673-1679出版社
AMER CHEMICAL SOC
DOI: 10.1021/acsnano.7b08316
关键词
TMV coat protein; self-assembly; protein crystal; crystal structure; protein interactions
类别
资金
- National Natural Science Foundation of China [11375256, 21673280, U1632265, 21425103]
- National Key Research and Development Program of China [2016YFA0101503]
In this work, a typical cylinder-shaped tobacco mosaic virus coat protein (TMVCP) is employed as an anisotropic building block to assemble into triclinic and hexagonal close-packed (HCP) protein crystals by introducing cysteine residues at the 1 and 3 sites and four histidine residues at the C-terminal, respectively. The engineered functional groups of cysteine and histidine in the TMVCP and the self-assembly conditions determine the thermodynamics and kinetics in the self-assembly process for forming different crystal structures. The results show that the TMVCPs are thermodynamically driven to form triclinic crystals due to the formation of disulfide bonds between neighboring TMVCPs. On the other hand, the self-assembly of HCP crystals is kinetically directed by the strong metal-histidine chelation. This work not only greatly expands TMVCP for fabricating promising nanomaterials but also represents an approach to adjusting the protein crystal structures by tuning the thermodynamics and kinetics during crystallization.
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