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Giant capsids from lattice self-assembly of cyclodextrin complexes
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 lattic...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5481833/ https://www.ncbi.nlm.nih.gov/pubmed/28631756 http://dx.doi.org/10.1038/ncomms15856 |
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author | Yang, Shenyu Yan, Yun Huang, Jianbin Petukhov, Andrei V. Kroon-Batenburg, Loes M. J. Drechsler, Markus Zhou, Chengcheng Tu, Mei Granick, Steve Jiang, Lingxiang |
author_facet | Yang, Shenyu Yan, Yun Huang, Jianbin Petukhov, Andrei V. Kroon-Batenburg, Loes M. J. Drechsler, Markus Zhou, Chengcheng Tu, Mei Granick, Steve Jiang, Lingxiang |
author_sort | Yang, Shenyu |
collection | PubMed |
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. |
format | Online Article Text |
id | pubmed-5481833 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-54818332017-07-06 Giant capsids from lattice self-assembly of cyclodextrin complexes Yang, Shenyu Yan, Yun Huang, Jianbin Petukhov, Andrei V. Kroon-Batenburg, Loes M. J. Drechsler, Markus Zhou, Chengcheng Tu, Mei Granick, Steve Jiang, Lingxiang Nat Commun Article 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. Nature Publishing Group 2017-06-20 /pmc/articles/PMC5481833/ /pubmed/28631756 http://dx.doi.org/10.1038/ncomms15856 Text en Copyright © 2017, The Author(s) http://creativecommons.org/licenses/by/4.0/ Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article Yang, Shenyu Yan, Yun Huang, Jianbin Petukhov, Andrei V. Kroon-Batenburg, Loes M. J. Drechsler, Markus Zhou, Chengcheng Tu, Mei Granick, Steve Jiang, Lingxiang Giant capsids from lattice self-assembly of cyclodextrin complexes |
title | Giant capsids from lattice self-assembly of cyclodextrin complexes |
title_full | Giant capsids from lattice self-assembly of cyclodextrin complexes |
title_fullStr | Giant capsids from lattice self-assembly of cyclodextrin complexes |
title_full_unstemmed | Giant capsids from lattice self-assembly of cyclodextrin complexes |
title_short | Giant capsids from lattice self-assembly of cyclodextrin complexes |
title_sort | giant capsids from lattice self-assembly of cyclodextrin complexes |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5481833/ https://www.ncbi.nlm.nih.gov/pubmed/28631756 http://dx.doi.org/10.1038/ncomms15856 |
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