Giant capsids from lattice self-assembly of cyclodextrin complexes.

Citation data:

Nature communications, ISSN: 2041-1723, Vol: 8, Page: 15856

Publication Year:
2017
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Repository URL:
https://www.nature.com/articles/ncomms15856
PMID:
28631756
DOI:
10.1038/ncomms15856
Author(s):
Yang, Shenyu; Yan, Yun; Huang, Jianbin; Petukhov, Andrei V; Kroon-Batenburg, Loes M J; Drechsler, Markus; Zhou, Chengcheng; Tu, Mei; Granick, Steve; Jiang, Lingxiang
Publisher(s):
Springer Nature
Tags:
Chemistry; Biochemistry, Genetics and Molecular Biology; Physics and Astronomy
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article description
Proteins can readily assemble into rigid, crystalline and functional structures such as viral capsids and bacterial compartments. Despite ongoing advances, it is still a fundamental challenge to design and synthesize protein-mimetic molecules to form crystalline structures. Here we report the lattice self-assembly of cyclodextrin complexes into a variety of capsid-like structures such as lamellae, helical tubes and hollow rhombic dodecahedra. The dodecahedral morphology has not hitherto been observed in self-assembly systems. The tubes can spontaneously encapsulate colloidal particles and liposomes. The dodecahedra and tubes are respectively comparable to and much larger than the largest known virus. In particular, the resemblance to protein assemblies is not limited to morphology but extends to structural rigidity and crystallinity-a well-defined, 2D rhombic lattice of molecular arrangement is strikingly universal for all the observed structures. We propose a simple design rule for the current lattice self-assembly, potentially opening doors for new protein-mimetic materials.