The Collagen Suprafamily: From Biosynthesis to Advanced Biomaterial Development.
collagen biomaterials
collagen characterization
collagen crosslinking
collagen self-assembly
extracellular matrix
Journal
Advanced materials (Deerfield Beach, Fla.)
ISSN: 1521-4095
Titre abrégé: Adv Mater
Pays: Germany
ID NLM: 9885358
Informations de publication
Date de publication:
Jan 2019
Jan 2019
Historique:
received:
14
03
2018
revised:
03
06
2018
pubmed:
21
8
2018
medline:
13
4
2019
entrez:
21
8
2018
Statut:
ppublish
Résumé
Collagen is the oldest and most abundant extracellular matrix protein that has found many applications in food, cosmetic, pharmaceutical, and biomedical industries. First, an overview of the family of collagens and their respective structures, conformation, and biosynthesis is provided. The advances and shortfalls of various collagen preparations (e.g., mammalian/marine extracted collagen, cell-produced collagens, recombinant collagens, and collagen-like peptides) and crosslinking technologies (e.g., chemical, physical, and biological) are then critically discussed. Subsequently, an array of structural, thermal, mechanical, biochemical, and biological assays is examined, which are developed to analyze and characterize collagenous structures. Lastly, a comprehensive review is provided on how advances in engineering, chemistry, and biology have enabled the development of bioactive, 3D structures (e.g., tissue grafts, biomaterials, cell-assembled tissue equivalents) that closely imitate native supramolecular assemblies and have the capacity to deliver in a localized and sustained manner viable cell populations and/or bioactive/therapeutic molecules. Clearly, collagens have a long history in both evolution and biotechnology and continue to offer both challenges and exciting opportunities in regenerative medicine as nature's biomaterial of choice.
Identifiants
pubmed: 30126066
doi: 10.1002/adma.201801651
doi:
Substances chimiques
Biocompatible Materials
0
Recombinant Proteins
0
Collagen
9007-34-5
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
e1801651Subventions
Organisme : Teagasc Walsh Fellowship
ID : 2014045
Organisme : ReValueProtein Research
ID : 11/F/043
Organisme : Department of Agriculture, Food and the Marine (DAFM) under the National Development Plan 2007-2013
Organisme : Irish Government
Organisme : Health Research Board, Health Research Awards Programme
ID : HRA_POR/2011/84
Organisme : Science Foundation Ireland
Organisme : Career Development Award Programme
ID : 15/CDA/3629
Organisme : Science Foundation Ireland
Organisme : European Regional Development Fund
ID : 13/RC/2073
Organisme : College of Engineering and Informatics, National University of Ireland Galway
Organisme : Green Nano Mesh Project
ID : 263289
Organisme : Neurograft Project
ID : 304936
Organisme : EU H2020
Organisme : Tendon Therapy Train Project
ID : 676338
Organisme : National University of Singapore Tissue Engineering Programme
Informations de copyright
© 2018 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.