| Literature DB >> 30126066 |
Anna Sorushanova1,2, Luis M Delgado1,2, Zhuning Wu1,2, Naledi Shologu1,2, Aniket Kshirsagar2, Rufus Raghunath3, Anne M Mullen4, Yves Bayon5, Abhay Pandit2, Michael Raghunath3, Dimitrios I Zeugolis1,2.
Abstract
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.Entities:
Keywords: collagen biomaterials; collagen characterization; collagen crosslinking; collagen self-assembly; extracellular matrix
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Year: 2018 PMID: 30126066 DOI: 10.1002/adma.201801651
Source DB: PubMed Journal: Adv Mater ISSN: 0935-9648 Impact factor: 30.849