Decorated networks of native proteins: nanomaterials with tunable mesoscopic domain size
| Autor: | Angelique Coutable-Pennarun, J. L. Ross Anderson, Ioatzin Rios de Anda, Annela M. Seddon, C. Patrick Royall, Stephen Whitelam, Christopher Brasnett, John Russo |
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| Rok vydání: | 2021 |
| Předmět: |
Computer science
BrisSynBio Nanotechnology 02 engineering and technology 010402 general chemistry 01 natural sciences Nanomaterials Domain (software engineering) Synthetic biology Component (UML) Denaturation (biochemistry) Soft matter Author Informa Mesoscopic physics Bristol BioDesign Institute Proteins General Chemistry 021001 nanoscience & nanotechnology Condensed Matter Physics Nanostructures 0104 chemical sciences Chemistry 0210 nano-technology mCherry |
| Zdroj: | Ríos de Anda, I, Coutable-Pennarun, A, Brasnett, C, Whitelam, S, Seddon, A, Russo, J, Anderson, J L R & Royall, C P 2021, ' Decorated networks of native proteins : nanomaterials with tunable mesoscopic domain size ', Soft Matter, vol. 17, no. 28, pp. 6873-6883 . https://doi.org/10.1039/d0sm02269a Soft matter 17 (2021): 6873–6883. doi:10.1039/d0sm02269a info:cnr-pdr/source/autori:Rios de Anda I.; Coutable-Pennarun A.; Brasnett C.; Whitelam S.; Seddon A.; Russo J.; Anderson J.L.R.; Royall C.P./titolo:Decorated networks of native proteins: nanomaterials with tunable mesoscopic domain size/doi:10.1039%2Fd0sm02269a/rivista:Soft matter (Print)/anno:2021/pagina_da:6873/pagina_a:6883/intervallo_pagine:6873–6883/volume:17 Soft Matter |
| ISSN: | 1744-6848 1744-683X |
| Popis: | 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. By controlling the specificity of salt–protein interactions, we designed a new protein self-assembly strategy, which yielded a novel binary network. Using fluorescent proteins, we obtained a backbone gel of eGFP, which was decorated in a controlled manner with mCherry. |
| Databáze: | OpenAIRE |
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