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Decorated networks of native proteins: nanomaterials with tunable mesoscopic domain size
Natural and artificial proteins with designer properties and functionalities offer unparalleled opportunity for functional nanoarchitectures formed through self-assembly. However, to exploit this potential we need to design the system such that assembly results in desired architecture forms while av...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Royal Society of Chemistry
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8294043/ https://www.ncbi.nlm.nih.gov/pubmed/34231559 http://dx.doi.org/10.1039/d0sm02269a |
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author | Ríos de Anda, Ioatzin Coutable-Pennarun, Angélique Brasnett, Christopher Whitelam, Stephen Seddon, Annela Russo, John Anderson, J. L. Ross Royall, C. Patrick |
author_facet | Ríos de Anda, Ioatzin Coutable-Pennarun, Angélique Brasnett, Christopher Whitelam, Stephen Seddon, Annela Russo, John Anderson, J. L. Ross Royall, C. Patrick |
author_sort | Ríos de Anda, Ioatzin |
collection | PubMed |
description | Natural and artificial proteins with designer properties and functionalities offer unparalleled opportunity for functional nanoarchitectures formed through self-assembly. However, to exploit this potential we need to design the system such that assembly results in desired architecture forms while avoiding denaturation and therefore retaining protein functionality. Here we address this challenge with a model system of fluorescent proteins. By manipulating self-assembly using techniques inspired by soft matter where interactions between the components are controlled to yield the desired structure, we have developed a methodology to assemble networks of proteins of one species which we can decorate with another, whose coverage we can tune. Consequently, the interfaces between domains of each component can also be tuned, with potential applications for example in energy – or electron – transfer. Our model system of eGFP and mCherry with tuneable interactions reveals control over domain sizes in the resulting networks. |
format | Online Article Text |
id | pubmed-8294043 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | The Royal Society of Chemistry |
record_format | MEDLINE/PubMed |
spelling | pubmed-82940432021-08-03 Decorated networks of native proteins: nanomaterials with tunable mesoscopic domain size Ríos de Anda, Ioatzin Coutable-Pennarun, Angélique Brasnett, Christopher Whitelam, Stephen Seddon, Annela Russo, John Anderson, J. L. Ross Royall, C. Patrick Soft Matter Chemistry Natural and artificial proteins with designer properties and functionalities offer unparalleled opportunity for functional nanoarchitectures formed through self-assembly. However, to exploit this potential we need to design the system such that assembly results in desired architecture forms while avoiding denaturation and therefore retaining protein functionality. Here we address this challenge with a model system of fluorescent proteins. By manipulating self-assembly using techniques inspired by soft matter where interactions between the components are controlled to yield the desired structure, we have developed a methodology to assemble networks of proteins of one species which we can decorate with another, whose coverage we can tune. Consequently, the interfaces between domains of each component can also be tuned, with potential applications for example in energy – or electron – transfer. Our model system of eGFP and mCherry with tuneable interactions reveals control over domain sizes in the resulting networks. The Royal Society of Chemistry 2021-06-30 /pmc/articles/PMC8294043/ /pubmed/34231559 http://dx.doi.org/10.1039/d0sm02269a Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by-nc/3.0/ |
spellingShingle | Chemistry Ríos de Anda, Ioatzin Coutable-Pennarun, Angélique Brasnett, Christopher Whitelam, Stephen Seddon, Annela Russo, John Anderson, J. L. Ross Royall, C. Patrick Decorated networks of native proteins: nanomaterials with tunable mesoscopic domain size |
title | Decorated networks of native proteins: nanomaterials with tunable mesoscopic domain size |
title_full | Decorated networks of native proteins: nanomaterials with tunable mesoscopic domain size |
title_fullStr | Decorated networks of native proteins: nanomaterials with tunable mesoscopic domain size |
title_full_unstemmed | Decorated networks of native proteins: nanomaterials with tunable mesoscopic domain size |
title_short | Decorated networks of native proteins: nanomaterials with tunable mesoscopic domain size |
title_sort | decorated networks of native proteins: nanomaterials with tunable mesoscopic domain size |
topic | Chemistry |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8294043/ https://www.ncbi.nlm.nih.gov/pubmed/34231559 http://dx.doi.org/10.1039/d0sm02269a |
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