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Kinetic Analysis Reveals the Role of Secondary Nucleation in Regenerated Silk Fibroin Self-Assembly
[Image: see text] Silk proteins obtained from the Bombyx mori silkworm have been extensively studied due to their remarkable mechanical properties. One of the major structural components of this complex material is silk fibroin, which can be isolated and processed further in vitro to form artificial...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2023
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10091410/ https://www.ncbi.nlm.nih.gov/pubmed/36926854 http://dx.doi.org/10.1021/acs.biomac.2c01479 |
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author | Kamada, Ayaka Toprakcioglu, Zenon Knowles, Tuomas P. J. |
author_facet | Kamada, Ayaka Toprakcioglu, Zenon Knowles, Tuomas P. J. |
author_sort | Kamada, Ayaka |
collection | PubMed |
description | [Image: see text] Silk proteins obtained from the Bombyx mori silkworm have been extensively studied due to their remarkable mechanical properties. One of the major structural components of this complex material is silk fibroin, which can be isolated and processed further in vitro to form artificial functional materials. Due to the excellent biocompatibility and rich self-assembly behavior, there has been sustained interest in such materials formed through the assembly of regenerated silk fibroin feedstocks. The molecular mechanisms by which the soluble regenerated fibroin molecules self-assemble into protein nanofibrils remain, however, largely unknown. Here, we use the framework of chemical kinetics to connect macroscopic measurements of regenerated silk fibroin self-assembly to the underlying microscopic mechanisms. Our results reveal that the aggregation of regenerated silk fibroin is dominated by a nonclassical secondary nucleation processes, where the formation of new fibrils is catalyzed by the existing aggregates in an autocatalytic manner. Such secondary nucleation pathways were originally discovered in the context of polymerization of disease-associated proteins, but the present results demonstrate that this pathway can also occur in functional assembly. Furthermore, our results show that shear flow induces the formation of nuclei, which subsequently accelerate the process of aggregation through an autocatalytic amplification driven by the secondary nucleation pathway. Taken together, these results allow us to identify the parameters governing the kinetics of regenerated silk fibroin self-assembly and expand our current understanding of the spinning of bioinspired protein-based fibers, which have a wide range of applications in materials science. |
format | Online Article Text |
id | pubmed-10091410 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | American Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-100914102023-04-13 Kinetic Analysis Reveals the Role of Secondary Nucleation in Regenerated Silk Fibroin Self-Assembly Kamada, Ayaka Toprakcioglu, Zenon Knowles, Tuomas P. J. Biomacromolecules [Image: see text] Silk proteins obtained from the Bombyx mori silkworm have been extensively studied due to their remarkable mechanical properties. One of the major structural components of this complex material is silk fibroin, which can be isolated and processed further in vitro to form artificial functional materials. Due to the excellent biocompatibility and rich self-assembly behavior, there has been sustained interest in such materials formed through the assembly of regenerated silk fibroin feedstocks. The molecular mechanisms by which the soluble regenerated fibroin molecules self-assemble into protein nanofibrils remain, however, largely unknown. Here, we use the framework of chemical kinetics to connect macroscopic measurements of regenerated silk fibroin self-assembly to the underlying microscopic mechanisms. Our results reveal that the aggregation of regenerated silk fibroin is dominated by a nonclassical secondary nucleation processes, where the formation of new fibrils is catalyzed by the existing aggregates in an autocatalytic manner. Such secondary nucleation pathways were originally discovered in the context of polymerization of disease-associated proteins, but the present results demonstrate that this pathway can also occur in functional assembly. Furthermore, our results show that shear flow induces the formation of nuclei, which subsequently accelerate the process of aggregation through an autocatalytic amplification driven by the secondary nucleation pathway. Taken together, these results allow us to identify the parameters governing the kinetics of regenerated silk fibroin self-assembly and expand our current understanding of the spinning of bioinspired protein-based fibers, which have a wide range of applications in materials science. American Chemical Society 2023-03-16 /pmc/articles/PMC10091410/ /pubmed/36926854 http://dx.doi.org/10.1021/acs.biomac.2c01479 Text en © 2023 The Authors. Published by American Chemical Society https://creativecommons.org/licenses/by/4.0/Permits the broadest form of re-use including for commercial purposes, provided that author attribution and integrity are maintained (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Kamada, Ayaka Toprakcioglu, Zenon Knowles, Tuomas P. J. Kinetic Analysis Reveals the Role of Secondary Nucleation in Regenerated Silk Fibroin Self-Assembly |
title | Kinetic Analysis
Reveals the Role of Secondary Nucleation
in Regenerated Silk Fibroin Self-Assembly |
title_full | Kinetic Analysis
Reveals the Role of Secondary Nucleation
in Regenerated Silk Fibroin Self-Assembly |
title_fullStr | Kinetic Analysis
Reveals the Role of Secondary Nucleation
in Regenerated Silk Fibroin Self-Assembly |
title_full_unstemmed | Kinetic Analysis
Reveals the Role of Secondary Nucleation
in Regenerated Silk Fibroin Self-Assembly |
title_short | Kinetic Analysis
Reveals the Role of Secondary Nucleation
in Regenerated Silk Fibroin Self-Assembly |
title_sort | kinetic analysis
reveals the role of secondary nucleation
in regenerated silk fibroin self-assembly |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10091410/ https://www.ncbi.nlm.nih.gov/pubmed/36926854 http://dx.doi.org/10.1021/acs.biomac.2c01479 |
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