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Nanoreactor Design Based on Self-Assembling Protein Nanocages

Self-assembling proteins that form diverse architectures are widely used in material science and nanobiotechnology. One class belongs to protein nanocages, which are compartments with nanosized internal spaces. Because of the precise nanoscale structures, proteinaceous compartments are ideal materia...

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Detalles Bibliográficos
Autores principales: Ren, Huimei, Zhu, Shaozhou, Zheng, Guojun
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6387247/
https://www.ncbi.nlm.nih.gov/pubmed/30704048
http://dx.doi.org/10.3390/ijms20030592
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author Ren, Huimei
Zhu, Shaozhou
Zheng, Guojun
author_facet Ren, Huimei
Zhu, Shaozhou
Zheng, Guojun
author_sort Ren, Huimei
collection PubMed
description Self-assembling proteins that form diverse architectures are widely used in material science and nanobiotechnology. One class belongs to protein nanocages, which are compartments with nanosized internal spaces. Because of the precise nanoscale structures, proteinaceous compartments are ideal materials for use as general platforms to create distinct microenvironments within confined cellular environments. This spatial organization strategy brings several advantages including the protection of catalyst cargo, faster turnover rates, and avoiding side reactions. Inspired by diverse molecular machines in nature, bioengineers have developed a variety of self-assembling supramolecular protein cages for use as biosynthetic nanoreactors that mimic natural systems. In this mini-review, we summarize current progress and ongoing efforts creating self-assembling protein based nanoreactors and their use in biocatalysis and synthetic biology. We also highlight the prospects for future research on these versatile nanomaterials.
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spelling pubmed-63872472019-02-27 Nanoreactor Design Based on Self-Assembling Protein Nanocages Ren, Huimei Zhu, Shaozhou Zheng, Guojun Int J Mol Sci Review Self-assembling proteins that form diverse architectures are widely used in material science and nanobiotechnology. One class belongs to protein nanocages, which are compartments with nanosized internal spaces. Because of the precise nanoscale structures, proteinaceous compartments are ideal materials for use as general platforms to create distinct microenvironments within confined cellular environments. This spatial organization strategy brings several advantages including the protection of catalyst cargo, faster turnover rates, and avoiding side reactions. Inspired by diverse molecular machines in nature, bioengineers have developed a variety of self-assembling supramolecular protein cages for use as biosynthetic nanoreactors that mimic natural systems. In this mini-review, we summarize current progress and ongoing efforts creating self-assembling protein based nanoreactors and their use in biocatalysis and synthetic biology. We also highlight the prospects for future research on these versatile nanomaterials. MDPI 2019-01-30 /pmc/articles/PMC6387247/ /pubmed/30704048 http://dx.doi.org/10.3390/ijms20030592 Text en © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Ren, Huimei
Zhu, Shaozhou
Zheng, Guojun
Nanoreactor Design Based on Self-Assembling Protein Nanocages
title Nanoreactor Design Based on Self-Assembling Protein Nanocages
title_full Nanoreactor Design Based on Self-Assembling Protein Nanocages
title_fullStr Nanoreactor Design Based on Self-Assembling Protein Nanocages
title_full_unstemmed Nanoreactor Design Based on Self-Assembling Protein Nanocages
title_short Nanoreactor Design Based on Self-Assembling Protein Nanocages
title_sort nanoreactor design based on self-assembling protein nanocages
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6387247/
https://www.ncbi.nlm.nih.gov/pubmed/30704048
http://dx.doi.org/10.3390/ijms20030592
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