Changes in the mechanical properties of dermal sheep collagen during in vitro degradation
- 1 February 1995
- journal article
- research article
- Published by Wiley in Journal of Biomedical Materials Research
- Vol. 29 (2) , 139-147
- https://doi.org/10.1002/jbm.820290202
Abstract
The changes in tensile strength, elongation at break, and high strain modulus of dermal sheep collagen (DSC) during in vitro degradation using bacterial collagenase were studied. The changes in mechanical properties were compared with the change in weight of the samples as a function of degradation time. DSC was crosslinked with either glutaraldehyde (GA) or hexamethylene diisocyanate (HMDIC). During degradation, the changes in mechanical properties of the N-DSC, H-DSC or G-DSC samples were more pronounced than the changes in the weight of the samples. Of the mechanical properties studied, the tensile strength was most susceptible to degradation of the DSC samples. After 2.5 h, N-DSC samples had lost only 55% of their initial weight, but the samples had no tensile strength left. Similar results were obtained for H-DSC, which retained no tensile strength after 24 h degradation, whereas only 45% of the initial weight was lost. G-DSC lost 3.5% of its weight after 24 h degradation, but only 25% of the initial tensile strength remained. © 1995 John Wiley & Sons, Inc.Keywords
This publication has 24 references indexed in Scilit:
- Macromolecular release from collagen monolithic devicesJournal of Biomedical Materials Research, 1990
- Preparation by direct metal exchange and kinetic study of active site metal substituted class I and class II Clostridium histolyticum collagenasesBiochemistry, 1988
- Chemically modified collagen: A natural biomaterial for tissue replacementJournal of Biomedical Materials Research, 1987
- Mechanism of crosslinking of proteins by glutaraldehyde III. Reaction with collagen in tissuesConnective Tissue Research, 1985
- Relationship between the individual collagenases of Clostridium histolyticum: evidence for evolution by gene duplicationBiochemistry, 1984
- Mechanism of Crosslinking of Proteins by Glutaraldehyde II. Reaction with Monomeric and Polymeric CollagenConnective Tissue Research, 1982
- Collagen-induced platelet aggregation and release. I effects of side-chain modifications and role of arginyl residuesBiochimica et Biophysica Acta (BBA) - General Subjects, 1978
- Collagen Films: Effect of Cross-Linking on Physical and Biological PropertiesBiomaterials, Medical Devices, and Artificial Organs, 1973
- The hydrolysis of poly (L‐prolyl‐glycyl‐L‐prolyl) by bacterial collagenaseBiopolymers, 1972
- Phase Transitions in Collagen and Gelatin Systems1Journal of the American Chemical Society, 1958