Abstract
Collagen is the most abundant protein in mammals, accounting for approximately one-third of the total protein in the human body. Thus, it is a logical choice for the creation of biomimetic environments, and there is a long history of using collagen matrices for various tissue engineering applications. However, from a biomaterial perspective, the use of collagen-only scaffolds is associated with many challenges. Namely, the mechanical properties of collagen matrices can be difficult to tune across a wide range of values, and collagen itself is not highly amenable to direct chemical modification without affecting its architecture or bioactivity. Thus, many approaches have been pursued to design scaffold environments that display critical features of collagen but enable improved tunability of physical and biological characteristics. This paper provides a brief overview of approaches that have been employed to create such engineered collagen matrices. Specifically, these approaches include blending of collagen with other natural or synthetic polymers, chemical modifications of denatured collagen, de novo creation of collagen-mimetic chains, and reductionist methods to incorporate collagen moieties into other materials. These advancements in the creation of tunable, engineered collagen matrices will continue to enable the interrogation of novel and increasingly complex biological questions.
Highlights
Collagen is ubiquitous throughout the animal kingdom and is the most prevalent protein in mammals
We aim to provide a novel contribution to the literature by applying a holistic view of the broad field of engineered collagen matrices, discussing a wide variety of approaches that have been taken in pursuit of such collagen-mimicking materials
Because these scaffolds present native, full-length collagen to cells, they offer similar advantages with respect to tissue engineering as described in Section 2—with the exception that blending with another native extracellular matrix (ECM) component can even further enhance their biochemical mimicry compared to collagen alone
Summary
Collagen is ubiquitous throughout the animal kingdom and is the most prevalent protein in mammals. To meet the needs of these diverse and specialized tissues, the different collagen types demonstrate varying structure, morphology and function Despite this diversity, all collagens exhibit a unifying feature that classifies molecules as belonging to the collagen family, namely a repeating Gly-X-Y motif (wherein X and Y may be substituted with any amino acid, but most frequently with proline and 4-hydroxyproline, respectively [6]). Fibroblasts play important roles in manufacturing the monomeric subunits that form collagen, with the secondary structure dependent on the amino acid sequence of the protein, along with essential post-translational modifications such as hydroxylation and glycosylation After these modifications, the pro-α chains self-assemble into a triple-helical procollagen molecule that is secreted by the fibroblasts to the extracellular environment, and pro-peptide extension pieces cleaved to yield collagen molecules [9,10,11]. We aim to provide a novel contribution to the literature by applying a holistic view of the broad field of engineered collagen matrices, discussing a wide variety of approaches that have been taken in pursuit of such collagen-mimicking materials
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
