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Production of a Novel, Self-Assembled, Collagenous Matrix Mimicking the Hierarchical Structure of Native Aligned Connective Tissue

Published online by Cambridge University Press:  15 February 2011

G. D. Pins
Affiliation:
University of Medicine and Dentistry of New Jersey - Robert Wood Johnson Medical School, Department of Pathology/Division of Biomaterials, 675 Hoes Lane, Piscataway, New Jersey 08854, [email protected]
D. L. Christiansen
Affiliation:
University of Medicine and Dentistry of New Jersey - Robert Wood Johnson Medical School, Department of Pathology/Division of Biomaterials, 675 Hoes Lane, Piscataway, New Jersey 08854, [email protected]
R. Patel
Affiliation:
University of Medicine and Dentistry of New Jersey - Robert Wood Johnson Medical School, Department of Pathology/Division of Biomaterials, 675 Hoes Lane, Piscataway, New Jersey 08854, [email protected]
F. H. Silver
Affiliation:
University of Medicine and Dentistry of New Jersey - Robert Wood Johnson Medical School, Department of Pathology/Division of Biomaterials, 675 Hoes Lane, Piscataway, New Jersey 08854, [email protected]
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Abstract

The primary goal of the biomaterials scientist and tissue engineer is to create a biocompatible implant which mimics the mechanical and morphological properties of the tissue being replaced. In vitro experimentation has documented the propensity of soluble type I collagen to self-assemble and form microscopic collagen fibrils with periodic banding analogous to native collagen fiber. Our laboratory has further investigated in vitro self-assembly by incorporating several of the “natural” processes into a multi-step fiber formation procedure which generates macroscopic collagen fiber from its molecular constituents. Results of uniaxial tensile tests and ultrastructural analyses indicate that these coextruded and stretched collagen fibers have mechanical properties and fibrillar substructure comparable to that observed in native collagen fiber.

Type
Research Article
Copyright
Copyright © Materials Research Society 1996

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References

1. Silver, F. H., Kato, Y. P., Ohno, M., and Wasserman, A. J., J Long-Term Eff. Med. Imp., 2 (2), 165 (1992).Google Scholar
2. Birk, D. E., Silver, F. H., and Trelstad, R. L., in: The Cell Biology of the Extracellular Matrix, 2nd edit., edited by Hay, E. D. (Plenum Press, New York, 1991), pp. 221254.Google Scholar
3. Gross, J., Highberger, J. H., and Schmitt, F. O., Proc. Soc. Exptl. Biol. Med., 80 462 (1952).Google Scholar
4. Jackson, D. S. and Fessler, J. H., Nature, 176 69 (1955).Google Scholar
5. Pins, G. D., Huang, E. K., Christiansen, D. L., and Silver, F. H., Journal of Applied Polymer Science, (Submitted 1995).Google Scholar
6. Silver, F. H. and Trelstad, R. L., J. Biol. Chem., 255 (19), 9427 (1980).Google Scholar
7. Wang, M.-C., Pins, G. D., and Silver, F. H., Biomats., 15 (7), 507 (1994).Google Scholar
8. Kato, Y. P., Christiansen, D. L., Hahn, R. A., Shieh, S.-J., Goldstein, J. D., and Silver, F. H., Biomats., 10 38 (1989).Google Scholar
9. Cassell, J. M., Mandelhern, L., and Roberts, D. E., J. Amer. Leather Chem. Assoc., 57 556 (1962).Google Scholar
10. Gelman, R. A., Poppke, D. C., and Piez, K. A., J. Biol. Chem., 254 (22), 11741 (1979).Google Scholar
11. Silver, F. H., Langley, K. H., and Trelstad, R. L., Biopolymers, 18 2523 (1979).Google Scholar
12. Trelstad, R. L., Hayashi, K., and Gross, J., Proc. Natl. Acad. Sci. USA, 73 4027 (1976).Google Scholar
13. Farber, G., Garg, A. K., Birk, D. E., and Silver, F. H., Int. J. Biol. Macromol., 8 37 (1986).Google Scholar