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Amyloid Self-Assembly of Lysozyme in Self-Crowded Conditions: The Formation of a Protein Oligomer Hydrogel
[Image: see text] A method is designed to quickly form protein hydrogels, based on the self-assembly of highly concentrated lysozyme solutions in acidic conditions. Their properties can be easily modulated by selecting the curing temperature. Molecular insights on the gelation pathway, derived by in...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2021
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8023603/ https://www.ncbi.nlm.nih.gov/pubmed/33600168 http://dx.doi.org/10.1021/acs.biomac.0c01652 |
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author | Catalini, Sara Perinelli, Diego R. Sassi, Paola Comez, Lucia Palmieri, Giovanni F. Morresi, Assunta Bonacucina, Giulia Foggi, Paolo Pucciarelli, Stefania Paolantoni, Marco |
author_facet | Catalini, Sara Perinelli, Diego R. Sassi, Paola Comez, Lucia Palmieri, Giovanni F. Morresi, Assunta Bonacucina, Giulia Foggi, Paolo Pucciarelli, Stefania Paolantoni, Marco |
author_sort | Catalini, Sara |
collection | PubMed |
description | [Image: see text] A method is designed to quickly form protein hydrogels, based on the self-assembly of highly concentrated lysozyme solutions in acidic conditions. Their properties can be easily modulated by selecting the curing temperature. Molecular insights on the gelation pathway, derived by in situ FTIR spectroscopy, are related to calorimetric and rheological results, providing a consistent picture on structure–property correlations. In these self-crowded samples, the thermal unfolding induces the rapid formation of amyloid aggregates, leading to temperature-dependent quasi-stationary levels of antiparallel cross β-sheet links, attributed to kinetically trapped oligomers. Upon subsequent cooling, thermoreversible hydrogels develop by the formation of interoligomer contacts. Through heating/cooling cycles, the starting solutions can be largely recovered back, due to oligomer-to-monomer dissociation and refolding. Overall, transparent protein hydrogels can be easily formed in self-crowding conditions and their properties explained, considering the formation of interconnected amyloid oligomers. This type of biomaterial might be relevant in different fields, along with analogous systems of a fibrillar nature more commonly considered. |
format | Online Article Text |
id | pubmed-8023603 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | American Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-80236032021-04-07 Amyloid Self-Assembly of Lysozyme in Self-Crowded Conditions: The Formation of a Protein Oligomer Hydrogel Catalini, Sara Perinelli, Diego R. Sassi, Paola Comez, Lucia Palmieri, Giovanni F. Morresi, Assunta Bonacucina, Giulia Foggi, Paolo Pucciarelli, Stefania Paolantoni, Marco Biomacromolecules [Image: see text] A method is designed to quickly form protein hydrogels, based on the self-assembly of highly concentrated lysozyme solutions in acidic conditions. Their properties can be easily modulated by selecting the curing temperature. Molecular insights on the gelation pathway, derived by in situ FTIR spectroscopy, are related to calorimetric and rheological results, providing a consistent picture on structure–property correlations. In these self-crowded samples, the thermal unfolding induces the rapid formation of amyloid aggregates, leading to temperature-dependent quasi-stationary levels of antiparallel cross β-sheet links, attributed to kinetically trapped oligomers. Upon subsequent cooling, thermoreversible hydrogels develop by the formation of interoligomer contacts. Through heating/cooling cycles, the starting solutions can be largely recovered back, due to oligomer-to-monomer dissociation and refolding. Overall, transparent protein hydrogels can be easily formed in self-crowding conditions and their properties explained, considering the formation of interconnected amyloid oligomers. This type of biomaterial might be relevant in different fields, along with analogous systems of a fibrillar nature more commonly considered. American Chemical Society 2021-02-18 2021-03-08 /pmc/articles/PMC8023603/ /pubmed/33600168 http://dx.doi.org/10.1021/acs.biomac.0c01652 Text en © 2021 American Chemical Society 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 | Catalini, Sara Perinelli, Diego R. Sassi, Paola Comez, Lucia Palmieri, Giovanni F. Morresi, Assunta Bonacucina, Giulia Foggi, Paolo Pucciarelli, Stefania Paolantoni, Marco Amyloid Self-Assembly of Lysozyme in Self-Crowded Conditions: The Formation of a Protein Oligomer Hydrogel |
title | Amyloid Self-Assembly of Lysozyme in Self-Crowded
Conditions: The Formation of a Protein Oligomer Hydrogel |
title_full | Amyloid Self-Assembly of Lysozyme in Self-Crowded
Conditions: The Formation of a Protein Oligomer Hydrogel |
title_fullStr | Amyloid Self-Assembly of Lysozyme in Self-Crowded
Conditions: The Formation of a Protein Oligomer Hydrogel |
title_full_unstemmed | Amyloid Self-Assembly of Lysozyme in Self-Crowded
Conditions: The Formation of a Protein Oligomer Hydrogel |
title_short | Amyloid Self-Assembly of Lysozyme in Self-Crowded
Conditions: The Formation of a Protein Oligomer Hydrogel |
title_sort | amyloid self-assembly of lysozyme in self-crowded
conditions: the formation of a protein oligomer hydrogel |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8023603/ https://www.ncbi.nlm.nih.gov/pubmed/33600168 http://dx.doi.org/10.1021/acs.biomac.0c01652 |
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