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Protein Adsorption Enhances Energy Dissipation in Networks of Lysozyme Amyloid Fibrils
[Image: see text] Hydrogels of amyloid fibrils are a versatile biomaterial for tissue engineering and other biomedical applications. Their suitability for these applications has been partly ascribed to their excellent and potentially engineerable rheological properties. However, while in biomedical...
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/PMC8223478/ https://www.ncbi.nlm.nih.gov/pubmed/34097425 http://dx.doi.org/10.1021/acs.langmuir.1c00657 |
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author | van Dalen, Maurice C. E. Vaneyck, Jonathan Semerdzhiev, Slav A. Karperien, Marcel Post, Janine N. Claessens, Mireille M. A. E. |
author_facet | van Dalen, Maurice C. E. Vaneyck, Jonathan Semerdzhiev, Slav A. Karperien, Marcel Post, Janine N. Claessens, Mireille M. A. E. |
author_sort | van Dalen, Maurice C. E. |
collection | PubMed |
description | [Image: see text] Hydrogels of amyloid fibrils are a versatile biomaterial for tissue engineering and other biomedical applications. Their suitability for these applications has been partly ascribed to their excellent and potentially engineerable rheological properties. However, while in biomedical applications the gels have to function in compositionally complex physiological solutions, their rheological behavior is typically only characterized in simple buffers. Here we show that the viscoelastic response of networks of amyloid fibrils of the protein lysozyme in biologically relevant solutions substantially differs from the response in simple buffers. We observe enhanced energy dissipation in both cell culture medium and synovial fluid. We attribute this energy dissipation to interactions of the amyloid fibrils with other molecules in these solutions and especially to the adsorption of the abundantly present protein serum albumin. This finding provides the basis for a better understanding of the performance of amyloid hydrogels in biomedical applications. |
format | Online Article Text |
id | pubmed-8223478 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | American
Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-82234782021-06-25 Protein Adsorption Enhances Energy Dissipation in Networks of Lysozyme Amyloid Fibrils van Dalen, Maurice C. E. Vaneyck, Jonathan Semerdzhiev, Slav A. Karperien, Marcel Post, Janine N. Claessens, Mireille M. A. E. Langmuir [Image: see text] Hydrogels of amyloid fibrils are a versatile biomaterial for tissue engineering and other biomedical applications. Their suitability for these applications has been partly ascribed to their excellent and potentially engineerable rheological properties. However, while in biomedical applications the gels have to function in compositionally complex physiological solutions, their rheological behavior is typically only characterized in simple buffers. Here we show that the viscoelastic response of networks of amyloid fibrils of the protein lysozyme in biologically relevant solutions substantially differs from the response in simple buffers. We observe enhanced energy dissipation in both cell culture medium and synovial fluid. We attribute this energy dissipation to interactions of the amyloid fibrils with other molecules in these solutions and especially to the adsorption of the abundantly present protein serum albumin. This finding provides the basis for a better understanding of the performance of amyloid hydrogels in biomedical applications. American Chemical Society 2021-06-07 2021-06-22 /pmc/articles/PMC8223478/ /pubmed/34097425 http://dx.doi.org/10.1021/acs.langmuir.1c00657 Text en © 2021 The Authors. Published by American Chemical Society Permits non-commercial access and re-use, provided that author attribution and integrity are maintained; but does not permit creation of adaptations or other derivative works (https://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | van Dalen, Maurice C. E. Vaneyck, Jonathan Semerdzhiev, Slav A. Karperien, Marcel Post, Janine N. Claessens, Mireille M. A. E. Protein Adsorption Enhances Energy Dissipation in Networks of Lysozyme Amyloid Fibrils |
title | Protein Adsorption Enhances Energy Dissipation in
Networks of Lysozyme Amyloid Fibrils |
title_full | Protein Adsorption Enhances Energy Dissipation in
Networks of Lysozyme Amyloid Fibrils |
title_fullStr | Protein Adsorption Enhances Energy Dissipation in
Networks of Lysozyme Amyloid Fibrils |
title_full_unstemmed | Protein Adsorption Enhances Energy Dissipation in
Networks of Lysozyme Amyloid Fibrils |
title_short | Protein Adsorption Enhances Energy Dissipation in
Networks of Lysozyme Amyloid Fibrils |
title_sort | protein adsorption enhances energy dissipation in
networks of lysozyme amyloid fibrils |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8223478/ https://www.ncbi.nlm.nih.gov/pubmed/34097425 http://dx.doi.org/10.1021/acs.langmuir.1c00657 |
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