Collagen-Based Electrospun Materials for Tissue Engineering: A Systematic Review

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Abstract

Collagen is a key component of the extracellular matrix (ECM) in organs and tissues throughout the body and is used for many tissue engineering applications. Electrospinning of collagen can produce scaffolds in a wide variety of shapes, fiber diameters and porosities to match that of the native ECM. This systematic review aims to pool data from available manuscripts on electrospun collagen and tissue engineering to provide insight into the connection between source material, solvent, crosslinking method and functional outcomes. D-banding was most often observed in electrospun collagen formed using collagen type I isolated from calfskin, often isolated within the laboratory, with short solution solubilization times. All physical and chemical methods of crosslinking utilized imparted resistance to degradation and increased strength. Cytotoxicity was observed at high concentrations of crosslinking agents and when abbreviated rinsing protocols were utilized. Collagen and collagen-based scaffolds were capable of forming engineered tissues in vitro and in vivo with high similarity to the native structures.

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Electrospinning: applications in drug delivery and tissue engineering.

Travis Sill, Horst von Recum (2008)

Despite its long history and some preliminary work in tissue engineering nearly 30 years ago, electrospinning has not gained widespread interest as a potential polymer processing technique for applications in tissue engineering and drug delivery until the last 5-10 years. This renewed interest can be attributed to electrospinning's relative ease of use, adaptability, and the ability to fabricate fibers with diameters on the nanometer size scale. Furthermore, the electrospinning process affords the opportunity to engineer scaffolds with micro to nanoscale topography and high porosity similar to the natural extracellular matrix (ECM). The inherently high surface to volume ratio of electrospun scaffolds can enhance cell attachment, drug loading, and mass transfer properties. Various materials can be electrospun including: biodegradable, non-degradable, and natural materials. Electrospun fibers can be oriented or arranged randomly, giving control over both the bulk mechanical properties and the biological response to the scaffold. Drugs ranging from antibiotics and anticancer agents to proteins, DNA, and RNA can be incorporated into electrospun scaffolds. Suspensions containing living cells have even been electrospun successfully. The applications of electrospinning in tissue engineering and drug delivery are nearly limitless. This review summarizes the most recent and state of the art work in electrospinning and its uses in tissue engineering and drug delivery.

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Electrospinning of Collagen Nanofibers

Gary E Wnek, David Simpson, Gary L. Bowlin … (2002)

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Hierarchical structure and nanomechanics of collagen microfibrils from the atomistic scale up.

Alfonso Gautieri, Markus J. Buehler, Alberto Redaelli … (2011)

Collagen constitutes one-third of the human proteome, providing mechanical stability, elasticity, and strength to organisms and is the prime construction material in biology. Collagen is also the dominating material in the extracellular matrix and its stiffness controls cell differentiation, growth, and pathology. However, the origin of the unique mechanical properties of collagenous tissues, and in particular its stiffness, extensibility, and nonlinear mechanical response at large deformation, remains unknown. By using X-ray diffraction data of a collagen fibril (Orgel, J. P. R. O. et al. Proc. Natl. Acad. Sci. 2006, 103, 9001) here we present an experimentally validated model of the nanomechanics of a collagen microfibril that incorporates the full biochemical details of the amino acid sequence of constituting molecules and the nanoscale molecular arrangement. We demonstrate by direct mechanical testing that hydrated (wet) collagen microfibrils feature a Young's modulus of ≈300 MPa at small, and ≈1.2 GPa at larger deformation in excess of 10% strain, which is in excellent agreement with experimental data. We find that dehydrated (dry) collagen microfibrils show a significantly increased Young's modulus of ≈1.8-2.25 GPa, which is in agreement with experimental measurements and owing to tighter molecular packing. Our results show that the unique mechanical properties of collagen microfibrils arise due to their hierarchical structure at the nanoscale, where key deformation mechanisms are straightening of twisted triple-helical molecules at small strains, followed by axial stretching and eventual molecular uncoiling. The establishment of a model of hierarchical deformation mechanisms explains the striking difference of the elastic modulus of collagen fibrils compared with single molecules, which is found in the range of 4.8 ± 2 GPa, or ≈10-20 times greater. We find that collagen molecules alone are not capable of providing the broad range of mechanical functionality required for physiological function of collagenous tissues. Rather, the existence of an array of deformation mechanisms, derived from the hierarchical makeup of the material, is critical to the material's ability to confer key mechanical properties, specifically large extensibility, strain hardening, and toughness, despite the limitation that collagenous materials are constructed from only few distinct amino acids. The atomistic model of collagen microfibril mechanics now enables the bottom-up elucidation of structure-property relationships in a broader class of collagen materials (e.g., tendon, bone, cornea), including studies of genetic disease where the incorporation of biochemical details is essential. The availability of a molecular-based model of collagen tissues may eventually result in novel nanomedicine approaches to develop treatments for a broad class of collagen diseases and the design of de novo biomaterials for regenerative medicine.

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Author and article information

Contributors

Gou-Jen Wang: Role: Academic Editor

Journal

Journal ID (nlm-ta): Bioengineering (Basel)

Journal ID (iso-abbrev): Bioengineering (Basel)

Journal ID (publisher-id): bioengineering

Title: Bioengineering

Publisher: MDPI

ISSN (Electronic): 2306-5354

Publication date (Electronic): 18 March 2021

Publication date Collection: March 2021

Volume: 8

Issue: 3

Electronic Location Identifier: 39

Affiliations

[1 ]Department of Materials Science and Engineering, The Ohio State University, Columbus, OH 43210, USA; Blackstone.38@ 123456osu.edu

[2 ]Department of Biomedical Engineering, The Ohio State University, Columbus, OH 43210, USA; gallentine.5@ 123456osu.edu

[3 ]Research Department, Shriners Hospitals for Children, Cincinnati, OH 45229, USA

Author notes

[* ]Correspondence: powell.299@ 123456osu.edu

Article

Publisher ID: bioengineering-08-00039

DOI: 10.3390/bioengineering8030039

PMC ID: 8003061

PubMed ID: 33803598

SO-VID: e3501dde-3192-40bf-97fe-71104da44c2a

License:

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/).

Collagen-Based Electrospun Materials for Tissue Engineering: A Systematic Review

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Abstract

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Electrospinning for biomedical applications

Most cited references 111

Electrospinning: applications in drug delivery and tissue engineering.

Electrospinning of Collagen Nanofibers

Hierarchical structure and nanomechanics of collagen microfibrils from the atomistic scale up.

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