Angele, Peter and Abke, Jochen and Kujat, R. and Faltermeier, H. and Schumann, Detlef and Nerlich, Michael and Kinner, B. and Englert, Carsten and Ruszczak, Z. and Mehrl, R. and Müller, Rainer (2004) Influence of different collagen species on physico-chemical properties of crosslinked collagen matrices. Biomaterials 25 (14), pp. 2831-2841.
Full text not available from this repository.
Collagen-based scaffolds are appealing products for the repair of cartilage defects using tissue engineering strategies. The present study investigated the species-related differences of collagen scaffolds with and without 1-ethyl-3-(3-dimethyl aminopropyl) carbodiimide/N-hydroxysuccinimide-crosslinking. Resistance against collagenase digestion, swelling ratio, amino acid sequence, shrinkage temp., ultrastructural matrix morphol., crosslinking d. and stress-strain characteristics were detd. to evaluate the physico-chem. properties of equine- and bovine-collagen-based scaffolds. Three-factor ANOVA anal. revealed a highly significant effect of collagen type, crosslinking and time on degrdn. of the collagen samples by collagenase treatment. Crosslinked equine collagen samples showed a significantly reduced swelling ratio compared to bovine collagen samples. The amino acid compn. of equine collagen revealed a higher amt. of hydroxylysine and lysine. Shrinkage temps. of non-crosslinked samples showed a significant difference between equine (60°) and bovine collagen (57°). Three-factor ANOVA anal. revealed a highly significant effect of collagen type, crosslinking and matrix condition on rupture strength measured by stress-strain anal. The ultrastructure, the crosslinking d. and the strain at rupture between collagen matrixes of both species showed no significant differences. For tissue engineering purposes, the higher enzymic stability, the higher form stability, as well as the lower risk of transmissible disease make the case for considering equine-based collagen. This study also indicates that results obtained for scaffolds based on a certain collagen species may not be transferable to scaffolds based on another, because of the differing physico-chem. properties.
|Institutions:||Chemistry and Pharmacy > Institut für Physikalische und Theoretische Chemie > Chair of Chemistry VI - Physical Chemistry (Solution Chemistry) > Prof. Dr. Werner Kunz|
|Keywords:||collagen crosslinking species difference|
|Subjects:||500 Science > 540 Chemistry & allied sciences|
|Refereed:||Yes, this version has been refereed|
|Created at the University of Regensburg:||Yes|
|Deposited On:||19 Jun 2012 08:00|
|Last Modified:||19 Jun 2012 08:00|
- ASCII Citation
- Dublin Core
- HTML Citation
- OAI-ORE Resource Map (Atom Format)
- OAI-ORE Resource Map (RDF Format)
- Reference Manager
- Simple Metadata
Literature of the same author
at publisher (via DOI)