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Ultrasound regulated flexible protein materials: Fabrication, structure and physical-biological properties
Ultrasound can be used in the biomaterial field due to its high efficiency, easy operation, no chemical treatment, repeatability and high level of control. In this work, we demonstrated that ultrasound is able to quickly regulate protein structure at the solution assembly stage to obtain the designe...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8560629/ https://www.ncbi.nlm.nih.gov/pubmed/34673337 http://dx.doi.org/10.1016/j.ultsonch.2021.105800 |
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author | Cai, Bowen Gu, Hanling Wang, Fang Printon, Kyle Gu, Zhenggui Hu, Xiao |
author_facet | Cai, Bowen Gu, Hanling Wang, Fang Printon, Kyle Gu, Zhenggui Hu, Xiao |
author_sort | Cai, Bowen |
collection | PubMed |
description | Ultrasound can be used in the biomaterial field due to its high efficiency, easy operation, no chemical treatment, repeatability and high level of control. In this work, we demonstrated that ultrasound is able to quickly regulate protein structure at the solution assembly stage to obtain the designed properties of protein-based materials. Silk fibroin proteins dissolved in a formic acid-CaCl(2) solution system were treated in an ultrasound with varying times and powers. By altering these variables, the silks physical properties and structures can be fine-tuned and the results were investigated with Fourier transform infrared spectroscopy (FTIR), X-ray diffraction (XRD), scanning electron microscopy (SEM), differential scanning calorimetry (DSC), thermogravimetric analysis (TGA), dynamic mechanical analysis (DMA), gas permeability and water contact angle measurements. Ultrasonic treatment aids the interactions between the calcium ions and silk molecular chains which leads to increased amounts of intermolecular β-sheets and α-helix. This unique structural change caused the silk film to be highly insoluble in water while also inducing a hydrophilic swelling property. The ultrasound-regulated silk materials also showed higher thermal stability, better biocompatibility and breathability, and favorable mechanical strength and flexibility. It was also possible to tune the enzymatic degradation rate and biological response (cell growth and proliferation) of protein materials by changing ultrasound parameters. This study provides a unique physical and non-contact material processing method for the wide applications of protein-based biomaterials. |
format | Online Article Text |
id | pubmed-8560629 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-85606292021-11-08 Ultrasound regulated flexible protein materials: Fabrication, structure and physical-biological properties Cai, Bowen Gu, Hanling Wang, Fang Printon, Kyle Gu, Zhenggui Hu, Xiao Ultrason Sonochem Original Research Article Ultrasound can be used in the biomaterial field due to its high efficiency, easy operation, no chemical treatment, repeatability and high level of control. In this work, we demonstrated that ultrasound is able to quickly regulate protein structure at the solution assembly stage to obtain the designed properties of protein-based materials. Silk fibroin proteins dissolved in a formic acid-CaCl(2) solution system were treated in an ultrasound with varying times and powers. By altering these variables, the silks physical properties and structures can be fine-tuned and the results were investigated with Fourier transform infrared spectroscopy (FTIR), X-ray diffraction (XRD), scanning electron microscopy (SEM), differential scanning calorimetry (DSC), thermogravimetric analysis (TGA), dynamic mechanical analysis (DMA), gas permeability and water contact angle measurements. Ultrasonic treatment aids the interactions between the calcium ions and silk molecular chains which leads to increased amounts of intermolecular β-sheets and α-helix. This unique structural change caused the silk film to be highly insoluble in water while also inducing a hydrophilic swelling property. The ultrasound-regulated silk materials also showed higher thermal stability, better biocompatibility and breathability, and favorable mechanical strength and flexibility. It was also possible to tune the enzymatic degradation rate and biological response (cell growth and proliferation) of protein materials by changing ultrasound parameters. This study provides a unique physical and non-contact material processing method for the wide applications of protein-based biomaterials. Elsevier 2021-10-16 /pmc/articles/PMC8560629/ /pubmed/34673337 http://dx.doi.org/10.1016/j.ultsonch.2021.105800 Text en © 2021 The Authors https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Original Research Article Cai, Bowen Gu, Hanling Wang, Fang Printon, Kyle Gu, Zhenggui Hu, Xiao Ultrasound regulated flexible protein materials: Fabrication, structure and physical-biological properties |
title | Ultrasound regulated flexible protein materials: Fabrication, structure and physical-biological properties |
title_full | Ultrasound regulated flexible protein materials: Fabrication, structure and physical-biological properties |
title_fullStr | Ultrasound regulated flexible protein materials: Fabrication, structure and physical-biological properties |
title_full_unstemmed | Ultrasound regulated flexible protein materials: Fabrication, structure and physical-biological properties |
title_short | Ultrasound regulated flexible protein materials: Fabrication, structure and physical-biological properties |
title_sort | ultrasound regulated flexible protein materials: fabrication, structure and physical-biological properties |
topic | Original Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8560629/ https://www.ncbi.nlm.nih.gov/pubmed/34673337 http://dx.doi.org/10.1016/j.ultsonch.2021.105800 |
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