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Amyloids as Building Blocks for Macroscopic Functional Materials: Designs, Applications and Challenges

Amyloids are self-assembled protein aggregates that take cross-β fibrillar morphology. Although some amyloid proteins are best known for their association with Alzheimer’s and Parkinson’s disease, many other amyloids are found across diverse organisms, from bacteria to humans, and they play vital fu...

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Detalles Bibliográficos
Autores principales: Li, Jingyao, Zhang, Fuzhong
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8508955/
https://www.ncbi.nlm.nih.gov/pubmed/34639037
http://dx.doi.org/10.3390/ijms221910698
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author Li, Jingyao
Zhang, Fuzhong
author_facet Li, Jingyao
Zhang, Fuzhong
author_sort Li, Jingyao
collection PubMed
description Amyloids are self-assembled protein aggregates that take cross-β fibrillar morphology. Although some amyloid proteins are best known for their association with Alzheimer’s and Parkinson’s disease, many other amyloids are found across diverse organisms, from bacteria to humans, and they play vital functional roles. The rigidity, chemical stability, high aspect ratio, and sequence programmability of amyloid fibrils have made them attractive candidates for functional materials with applications in environmental sciences, material engineering, and translational medicines. This review focuses on recent advances in fabricating various types of macroscopic functional amyloid materials. We discuss different design strategies for the fabrication of amyloid hydrogels, high-strength materials, composite materials, responsive materials, extracellular matrix mimics, conductive materials, and catalytic materials.
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spelling pubmed-85089552021-10-13 Amyloids as Building Blocks for Macroscopic Functional Materials: Designs, Applications and Challenges Li, Jingyao Zhang, Fuzhong Int J Mol Sci Review Amyloids are self-assembled protein aggregates that take cross-β fibrillar morphology. Although some amyloid proteins are best known for their association with Alzheimer’s and Parkinson’s disease, many other amyloids are found across diverse organisms, from bacteria to humans, and they play vital functional roles. The rigidity, chemical stability, high aspect ratio, and sequence programmability of amyloid fibrils have made them attractive candidates for functional materials with applications in environmental sciences, material engineering, and translational medicines. This review focuses on recent advances in fabricating various types of macroscopic functional amyloid materials. We discuss different design strategies for the fabrication of amyloid hydrogels, high-strength materials, composite materials, responsive materials, extracellular matrix mimics, conductive materials, and catalytic materials. MDPI 2021-10-02 /pmc/articles/PMC8508955/ /pubmed/34639037 http://dx.doi.org/10.3390/ijms221910698 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Li, Jingyao
Zhang, Fuzhong
Amyloids as Building Blocks for Macroscopic Functional Materials: Designs, Applications and Challenges
title Amyloids as Building Blocks for Macroscopic Functional Materials: Designs, Applications and Challenges
title_full Amyloids as Building Blocks for Macroscopic Functional Materials: Designs, Applications and Challenges
title_fullStr Amyloids as Building Blocks for Macroscopic Functional Materials: Designs, Applications and Challenges
title_full_unstemmed Amyloids as Building Blocks for Macroscopic Functional Materials: Designs, Applications and Challenges
title_short Amyloids as Building Blocks for Macroscopic Functional Materials: Designs, Applications and Challenges
title_sort amyloids as building blocks for macroscopic functional materials: designs, applications and challenges
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8508955/
https://www.ncbi.nlm.nih.gov/pubmed/34639037
http://dx.doi.org/10.3390/ijms221910698
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