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Current Progress in Cross-Linked Peptide Self-Assemblies

Peptide-based fibrous supramolecular assemblies represent an emerging class of biomaterials that can realize various bioactivities and structures. Recently, a variety of peptide fibers with attractive functions have been designed together with the discovery of many peptide-based self-assembly units....

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Detalles Bibliográficos
Autores principales: Uchida, Noriyuki, Muraoka, Takahiro
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7589166/
https://www.ncbi.nlm.nih.gov/pubmed/33066439
http://dx.doi.org/10.3390/ijms21207577
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author Uchida, Noriyuki
Muraoka, Takahiro
author_facet Uchida, Noriyuki
Muraoka, Takahiro
author_sort Uchida, Noriyuki
collection PubMed
description Peptide-based fibrous supramolecular assemblies represent an emerging class of biomaterials that can realize various bioactivities and structures. Recently, a variety of peptide fibers with attractive functions have been designed together with the discovery of many peptide-based self-assembly units. Cross-linking of the peptide fibers is a key strategy to improve the functions of these materials. The cross-linking of peptide fibers forming three-dimensional networks in a dispersion can lead to changes in physical and chemical properties. Hydrogelation is a typical change caused by cross-linking, which makes it applicable to biomaterials such as cell scaffold materials. Cross-linking methods, which have been conventionally developed using water-soluble covalent polymers, are also useful in supramolecular peptide fibers. In the case of peptide fibers, unique cross-linking strategies can be designed by taking advantage of the functions of amino acids. This review focuses on the current progress in the design of cross-linked peptide fibers and their applications.
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spelling pubmed-75891662020-10-29 Current Progress in Cross-Linked Peptide Self-Assemblies Uchida, Noriyuki Muraoka, Takahiro Int J Mol Sci Review Peptide-based fibrous supramolecular assemblies represent an emerging class of biomaterials that can realize various bioactivities and structures. Recently, a variety of peptide fibers with attractive functions have been designed together with the discovery of many peptide-based self-assembly units. Cross-linking of the peptide fibers is a key strategy to improve the functions of these materials. The cross-linking of peptide fibers forming three-dimensional networks in a dispersion can lead to changes in physical and chemical properties. Hydrogelation is a typical change caused by cross-linking, which makes it applicable to biomaterials such as cell scaffold materials. Cross-linking methods, which have been conventionally developed using water-soluble covalent polymers, are also useful in supramolecular peptide fibers. In the case of peptide fibers, unique cross-linking strategies can be designed by taking advantage of the functions of amino acids. This review focuses on the current progress in the design of cross-linked peptide fibers and their applications. MDPI 2020-10-14 /pmc/articles/PMC7589166/ /pubmed/33066439 http://dx.doi.org/10.3390/ijms21207577 Text en © 2020 by the authors. 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 (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Uchida, Noriyuki
Muraoka, Takahiro
Current Progress in Cross-Linked Peptide Self-Assemblies
title Current Progress in Cross-Linked Peptide Self-Assemblies
title_full Current Progress in Cross-Linked Peptide Self-Assemblies
title_fullStr Current Progress in Cross-Linked Peptide Self-Assemblies
title_full_unstemmed Current Progress in Cross-Linked Peptide Self-Assemblies
title_short Current Progress in Cross-Linked Peptide Self-Assemblies
title_sort current progress in cross-linked peptide self-assemblies
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7589166/
https://www.ncbi.nlm.nih.gov/pubmed/33066439
http://dx.doi.org/10.3390/ijms21207577
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