Angele, Peter and Abke, Jochen and Kujat, Richard and Faltermeier, Hubert and Schumann, Detlef and Nerlich, Michael and Kinner, Bernd and Englert, Carsten and Ruszczak, Zbigniew and Mehrl, Robert and Mueller, Rainer (2004) Influence of different collagen species on physico-chemical properties of crosslinked collagen matrices. BIOMATERIALS, 25 (14). pp. 2831-2841. ISSN 0142-9612, 1878-5905
Full text not available from this repository. (Request a copy)Abstract
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 (EDC)/N-hydroxysuccinimide (NHS)-crosslinking. Resistance against collagenase digestion, swelling ratio, amino acid sequence, shrinkage temperature, ultrastructural matrix morphology, crosslinking density and stress-strain characteristics were determined to evaluate the physico-chemical properties of equine- and bovine-collagen-based scaffolds. Three-factor ANOVA analysis revealed a highly significant effect of collagen type (p = 0.0001), crosslinking (p = 0.0001) and time (p = 0.0001) on degradation of the collagen samples by collagenase treatment. Crosslinked equine collagen samples showed a significantly reduced swelling ratio compared to bovine collagen samples (p < 0.0001). The amino acid composition of equine collagen revealed a higher amount of hydroxylysine and lysine. Shrinkage temperatures of non-crosslinked samples showed a significant difference between equine (60degreesC) and bovine collagen (57 degreesC). Three-factor ANOVA analysis revealed a highly significant effect of collagen type (p = 0.0001), crosslinking (p = 0.0001) and matrix condition (h = 0.0001) on rupture strength treasured by stress-strain analysis. The ultrastructure. the crosslinking density and the strain at rupture between collagen matrices of both species showed no significant differences. For tissue engineering purposes, the higher enzymatic 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 physicochemical properties. (C) 2003 Elsevier Ltd. All rights reserved.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | DERMAL SHEEP COLLAGENS; ARTICULAR-CARTILAGE DEFECTS; IN-VITRO; CONTRACTILE BEHAVIOR; GAG MATRICES; CANINE CHONDROCYTES; PHYSICAL-PROPERTIES; LINKING TREATMENTS; CELLS; CARBODIIMIDE; crosslinking; collagen; tissue engineering; DSC; degradation; mechanical properties |
| Subjects: | 500 Science > 540 Chemistry & allied sciences 600 Technology > 610 Medical sciences Medicine |
| Divisions: | Medicine > Lehrstuhl für Unfallchirurgie Chemistry and Pharmacy > Institut für Physikalische und Theoretische Chemie |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 14 Jul 2021 05:18 |
| Last Modified: | 14 Jul 2021 05:18 |
| URI: | https://pred.uni-regensburg.de/id/eprint/37558 |
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