Tensile Mechanical Properties of Three-Dimensional Type I Collagen Extracellular Matrices With Varied Microstructure
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- 29 March 2002
- journal article
- research article
- Published by ASME International in Journal of Biomechanical Engineering
- Vol. 124 (2) , 214-222
- https://doi.org/10.1115/1.1449904
Abstract
The importance and priority of specific micro-structural and mechanical design parameters must be established to effectively engineer scaffolds (biomaterials) that mimic the extracellular matrix (ECM) environment of cells and have clinical applications as tissue substitutes. In this study, three-dimensional (3-D) matrices were prepared from type I collagen, the predominant compositional and structural component of connective tissue ECMs, and structural-mechanical relationships were studied. Polymerization conditions, including collagen concentration (0.3–3 mg/mL) and pH (6–9), were varied to obtain matrices of collagen fibrils with different microstructures. Confocal reflection microscopy was used to assess specific micro-structural features (e.g., diameter and length) and organization of component fibrils in 3-D. Microstructural analyses revealed that changes in collagen concentration affected fibril density while maintaining a relatively constant fibril diameter. On the other hand, both fibril length and diameter were affected by the pH of the polymerization reaction. Mechanically, all matrices exhibited a similar stress-strain curve with identifiable “toe,” “linear,” and “failure” regions. However, the linear modulus and failure stress increased with collagen concentration and were correlated with an increase in fibril density. Additionally, both the linear modulus and failure stress showed an increase with pH, which was related to an increased fibril length and a decreased fibril diameter. The tensile mechanical properties of the collagen matrices also showed strain rate dependence. Such fundamental information regarding the 3-D microstructural-mechanical properties of the ECM and its component molecules are important to our overall understanding of cell-ECM interactions (e.g., mechanotransduction) and the development of novel strategies for tissue repair and replacement.Keywords
This publication has 37 references indexed in Scilit:
- Small Intestinal Submucosa: A Tissue-Derived Extracellular Matrix That Promotes Tissue-Specific Growth and Differentiation of Cellsin VitroTissue Engineering, 1998
- Self-assembly of collagen fibers. Influence of fibrillar alignment and decorin on mechanical propertiesBiophysical Journal, 1997
- Rheology of reconstituted type I collagen gel in confined compressionJournal of Rheology, 1997
- Pore strain behaviour of collagen-glycosaminoglycan analogues of extracellular matrixBiomaterials, 1995
- Optimization of extruded collagen fibers for ACL reconstructionJournal of Biomedical Materials Research, 1993
- Re-freeze dried bilayer artificial skinBiomaterials, 1993
- Isometric contraction by fibroblasts and endothelial cells in tissue culture: a quantitative studyThe Journal of cell biology, 1992
- Influence of glycosaminoglycans on the collagen sponge component of a bilayer artificial skinBiomaterials, 1990
- Student research award in the hospital intern, resident or clinical fellow category, 15th annual meeting of the society for biomaterials, Lake Buena Vista, Florida, April 28–May 2, 1989. An evaluation of purified reconstituted type 1 collagen fibersJournal of Biomedical Materials Research, 1989
- Characterization of nuclei in in vitro collagen fibril formationBiopolymers, 1977