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Chemical unfolding of protein domains induces shape change in programmed protein hydrogels
Programmable behavior combined with tailored stiffness and tunable biomechanical response are key requirements for developing successful materials. However, these properties are still an elusive goal for protein-based biomaterials. Here, we use protein-polymer interactions to manipulate the stiffnes...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6884551/ https://www.ncbi.nlm.nih.gov/pubmed/31784506 http://dx.doi.org/10.1038/s41467-019-13312-0 |
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author | Khoury, Luai R. Popa, Ionel |
author_facet | Khoury, Luai R. Popa, Ionel |
author_sort | Khoury, Luai R. |
collection | PubMed |
description | Programmable behavior combined with tailored stiffness and tunable biomechanical response are key requirements for developing successful materials. However, these properties are still an elusive goal for protein-based biomaterials. Here, we use protein-polymer interactions to manipulate the stiffness of protein-based hydrogels made from bovine serum albumin (BSA) by using polyelectrolytes such as polyethyleneimine (PEI) and poly-L-lysine (PLL) at various concentrations. This approach confers protein-hydrogels with tunable wide-range stiffness, from ~10–64 kPa, without affecting the protein mechanics and nanostructure. We use the 6-fold increase in stiffness induced by PEI to program BSA hydrogels in various shapes. By utilizing the characteristic protein unfolding we can induce reversible shape-memory behavior of these composite materials using chemical denaturing solutions. The approach demonstrated here, based on protein engineering and polymer reinforcing, may enable the development and investigation of smart biomaterials and extend protein hydrogel capabilities beyond their conventional applications. |
format | Online Article Text |
id | pubmed-6884551 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-68845512019-12-03 Chemical unfolding of protein domains induces shape change in programmed protein hydrogels Khoury, Luai R. Popa, Ionel Nat Commun Article Programmable behavior combined with tailored stiffness and tunable biomechanical response are key requirements for developing successful materials. However, these properties are still an elusive goal for protein-based biomaterials. Here, we use protein-polymer interactions to manipulate the stiffness of protein-based hydrogels made from bovine serum albumin (BSA) by using polyelectrolytes such as polyethyleneimine (PEI) and poly-L-lysine (PLL) at various concentrations. This approach confers protein-hydrogels with tunable wide-range stiffness, from ~10–64 kPa, without affecting the protein mechanics and nanostructure. We use the 6-fold increase in stiffness induced by PEI to program BSA hydrogels in various shapes. By utilizing the characteristic protein unfolding we can induce reversible shape-memory behavior of these composite materials using chemical denaturing solutions. The approach demonstrated here, based on protein engineering and polymer reinforcing, may enable the development and investigation of smart biomaterials and extend protein hydrogel capabilities beyond their conventional applications. Nature Publishing Group UK 2019-11-29 /pmc/articles/PMC6884551/ /pubmed/31784506 http://dx.doi.org/10.1038/s41467-019-13312-0 Text en © The Author(s) 2019 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Khoury, Luai R. Popa, Ionel Chemical unfolding of protein domains induces shape change in programmed protein hydrogels |
title | Chemical unfolding of protein domains induces shape change in programmed protein hydrogels |
title_full | Chemical unfolding of protein domains induces shape change in programmed protein hydrogels |
title_fullStr | Chemical unfolding of protein domains induces shape change in programmed protein hydrogels |
title_full_unstemmed | Chemical unfolding of protein domains induces shape change in programmed protein hydrogels |
title_short | Chemical unfolding of protein domains induces shape change in programmed protein hydrogels |
title_sort | chemical unfolding of protein domains induces shape change in programmed protein hydrogels |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6884551/ https://www.ncbi.nlm.nih.gov/pubmed/31784506 http://dx.doi.org/10.1038/s41467-019-13312-0 |
work_keys_str_mv | AT khouryluair chemicalunfoldingofproteindomainsinducesshapechangeinprogrammedproteinhydrogels AT popaionel chemicalunfoldingofproteindomainsinducesshapechangeinprogrammedproteinhydrogels |