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Filming protein fibrillogenesis in real time

Protein fibrillogenesis is a universal tool of nano-to-micro scale construction supporting different forms of biological function. Its exploitable potential in nanoscience and technology is substantial, but the direct observation of homogeneous fibre growth able to underpin a kinetic-based rationale...

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Detalles Bibliográficos
Autores principales: Bella, Angelo, Shaw, Michael, Ray, Santanu, Ryadnov, Maxim G.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4269891/
https://www.ncbi.nlm.nih.gov/pubmed/25519825
http://dx.doi.org/10.1038/srep07529
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author Bella, Angelo
Shaw, Michael
Ray, Santanu
Ryadnov, Maxim G.
author_facet Bella, Angelo
Shaw, Michael
Ray, Santanu
Ryadnov, Maxim G.
author_sort Bella, Angelo
collection PubMed
description Protein fibrillogenesis is a universal tool of nano-to-micro scale construction supporting different forms of biological function. Its exploitable potential in nanoscience and technology is substantial, but the direct observation of homogeneous fibre growth able to underpin a kinetic-based rationale for building customized nanostructures in situ is lacking. Here we introduce a kinetic model of de novo protein fibrillogenesis which we imaged at the nanoscale and in real time, filmed. The model helped to reveal that, in contrast to heterogeneous amyloid assemblies, homogeneous protein recruitment is principally characterized by uniform rates of cooperative growth at both ends of growing fibers, bi-directional growth, with lateral growth arrested at a post-seeding stage. The model provides a foundation for in situ engineering of sequence-prescribed fibrous architectures.
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spelling pubmed-42698912014-12-30 Filming protein fibrillogenesis in real time Bella, Angelo Shaw, Michael Ray, Santanu Ryadnov, Maxim G. Sci Rep Article Protein fibrillogenesis is a universal tool of nano-to-micro scale construction supporting different forms of biological function. Its exploitable potential in nanoscience and technology is substantial, but the direct observation of homogeneous fibre growth able to underpin a kinetic-based rationale for building customized nanostructures in situ is lacking. Here we introduce a kinetic model of de novo protein fibrillogenesis which we imaged at the nanoscale and in real time, filmed. The model helped to reveal that, in contrast to heterogeneous amyloid assemblies, homogeneous protein recruitment is principally characterized by uniform rates of cooperative growth at both ends of growing fibers, bi-directional growth, with lateral growth arrested at a post-seeding stage. The model provides a foundation for in situ engineering of sequence-prescribed fibrous architectures. Nature Publishing Group 2014-12-18 /pmc/articles/PMC4269891/ /pubmed/25519825 http://dx.doi.org/10.1038/srep07529 Text en Copyright © 2014, Macmillan Publishers Limited. All rights reserved http://creativecommons.org/licenses/by-nc-nd/4.0/ This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivs 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder in order to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-nd/4.0/
spellingShingle Article
Bella, Angelo
Shaw, Michael
Ray, Santanu
Ryadnov, Maxim G.
Filming protein fibrillogenesis in real time
title Filming protein fibrillogenesis in real time
title_full Filming protein fibrillogenesis in real time
title_fullStr Filming protein fibrillogenesis in real time
title_full_unstemmed Filming protein fibrillogenesis in real time
title_short Filming protein fibrillogenesis in real time
title_sort filming protein fibrillogenesis in real time
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4269891/
https://www.ncbi.nlm.nih.gov/pubmed/25519825
http://dx.doi.org/10.1038/srep07529
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