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The physical basis of fabrication of amyloid-based hydrogels by lysozyme

The fabrication of amyloid-based hydrogels has attracted remarkable attention within the field of materials science and technology. These materials have a multitude of potential applications in the biomaterials field such as developing scaffolds for tissue engineering, drug delivery and hygiene prod...

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Autores principales: Kumari, Anumita, Ahmad, Basir
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Royal Society of Chemistry 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9075597/
https://www.ncbi.nlm.nih.gov/pubmed/35542254
http://dx.doi.org/10.1039/c9ra07179b
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author Kumari, Anumita
Ahmad, Basir
author_facet Kumari, Anumita
Ahmad, Basir
author_sort Kumari, Anumita
collection PubMed
description The fabrication of amyloid-based hydrogels has attracted remarkable attention within the field of materials science and technology. These materials have a multitude of potential applications in the biomaterials field such as developing scaffolds for tissue engineering, drug delivery and hygiene products. Despite the potential new applications of these materials, the physical nature of their assembly is not well understood. In this study, we have investigated how the conformation of the amyloid precursor state (I) is formed and correlated with the assembly of amyloid-based hydrogels. A transparent hydrogel was fabricated at pH 7.4 by cooling of the temperature-induced unfolded state of hen egg white lysozyme (HEWL). The completely unfolded state (U) at the gelation concentration of HEWL was obtained around 90 °C in the presence of tris(2-carboxyethyl)phosphine (TCEP), with a TCEP/HEWL molar ratio of 4 : 1. The characterization of the hydrogel showed that it was composed of an amyloid fibril-like material. The physical nature of its assembly was examined in detail and it was found that the hydrogel formation reaction was a three-step, four-states process (U → I → F → H). We concluded that the properties of the pre-molten globule state (I) of the protein correlated only with the fibrillation process, whereas the assembly of the fibrils into an hydrogel was found to be almost independent of the I state. Thus, the study presented here provides a complete biophysical insight into the pathway of lysozyme hydrogel assembly.
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spelling pubmed-90755972022-05-09 The physical basis of fabrication of amyloid-based hydrogels by lysozyme Kumari, Anumita Ahmad, Basir RSC Adv Chemistry The fabrication of amyloid-based hydrogels has attracted remarkable attention within the field of materials science and technology. These materials have a multitude of potential applications in the biomaterials field such as developing scaffolds for tissue engineering, drug delivery and hygiene products. Despite the potential new applications of these materials, the physical nature of their assembly is not well understood. In this study, we have investigated how the conformation of the amyloid precursor state (I) is formed and correlated with the assembly of amyloid-based hydrogels. A transparent hydrogel was fabricated at pH 7.4 by cooling of the temperature-induced unfolded state of hen egg white lysozyme (HEWL). The completely unfolded state (U) at the gelation concentration of HEWL was obtained around 90 °C in the presence of tris(2-carboxyethyl)phosphine (TCEP), with a TCEP/HEWL molar ratio of 4 : 1. The characterization of the hydrogel showed that it was composed of an amyloid fibril-like material. The physical nature of its assembly was examined in detail and it was found that the hydrogel formation reaction was a three-step, four-states process (U → I → F → H). We concluded that the properties of the pre-molten globule state (I) of the protein correlated only with the fibrillation process, whereas the assembly of the fibrils into an hydrogel was found to be almost independent of the I state. Thus, the study presented here provides a complete biophysical insight into the pathway of lysozyme hydrogel assembly. The Royal Society of Chemistry 2019-11-15 /pmc/articles/PMC9075597/ /pubmed/35542254 http://dx.doi.org/10.1039/c9ra07179b Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by/3.0/
spellingShingle Chemistry
Kumari, Anumita
Ahmad, Basir
The physical basis of fabrication of amyloid-based hydrogels by lysozyme
title The physical basis of fabrication of amyloid-based hydrogels by lysozyme
title_full The physical basis of fabrication of amyloid-based hydrogels by lysozyme
title_fullStr The physical basis of fabrication of amyloid-based hydrogels by lysozyme
title_full_unstemmed The physical basis of fabrication of amyloid-based hydrogels by lysozyme
title_short The physical basis of fabrication of amyloid-based hydrogels by lysozyme
title_sort physical basis of fabrication of amyloid-based hydrogels by lysozyme
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9075597/
https://www.ncbi.nlm.nih.gov/pubmed/35542254
http://dx.doi.org/10.1039/c9ra07179b
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