Duan, Y. (2007) An investigation of the effects of crosslinking of collagen on cell/collagen-matrix interaction. Doctoral thesis. The University of Northampton.
| Item Type: | Thesis (Doctoral) |
|---|---|
| Abstract: | Wound dressing plays an important role in wound recovery and collagen interacts with the human body in such a way that it has specific advantages compared to synthetic materials. The aim of the present study was to get an optimal crosslinking agent for collagen and so the mechanical, chemical and biochemical properties of crosslinked collagen materials were investigated. Fibroblast cells are important in the process of wound healing, so the interaction of human fibroblast cells with crosslinked collagen films were investigated as well. Collagen I was isolated from bovine achilles tendons and collagen films were formed using the isolated collagen I solution. Collagen films were crosslinked with glutaraldehyde (GA), genipin, hexamethylenediisocyanate (HMDC), 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide (EDC) at the equal concentration of 0.02 M and these crosslinked collagen films were compared with uncrosslinked collagen films (control). The surfaces of the crosslinked films were investigated using scanning electron microscopy (SEM). There was observable fibre structure on GA- and genipin-crosslinked collagen films. The tensile strength, elongation at break and low strain modulus of the crosslinked collagen films were investigated. The results showed that GA-, genipin- and HMDC-crosslinked collagen films obtained higher tensile strength than the control. Elongation at break of all the crosslinked collagen films became lower than the control. GA- and genipin-crosslinked collagen films obtained higher low strain modulus than other crosslinked collagen films and the control. The denaturation temperatures of all crosslinked collagen films were significantly higher than the control and the denaturation temperatures of GA- and genipin-crosslinked films were much higher than those of HMDC- and EDC-crosslinked films. All the crosslinked collagen films were resistant to the digestion of collagenase. These results suggest that all the crosslinking agents are effective and GA- and genipin-crosslinked films obtained more extensive crosslinking. The interaction of crosslinked collagen films with fibroblast cells was investigated, e.g. adhesion, proliferation and migration of fibroblast cells. The results demonstrated that the control, genipin- and EDC-crosslinked collagen films were conducive to cell adhesion. Fibroblast cells on the control, genipin- and EDC-crosslinked collagen films were able to proliferate after 24 hours, with increased growth after 48 hours. The fibroblast cells on the control, genipin- and EDC-crosslinked collagen films migrated directionally. The cells on genipin-crosslinked film initiated directional migration earlier than those on control- and EDC-crosslinked films. In summary, genipin crosslinked collagen films show high denaturation temperature, higher tensile strength and good biocompatibility for fibroblast cells adhesion, proliferation and migration. Genipin should be regarded as a suitable crosslinking agent for reconstituted collagen for use in wound dressing. |
| Subjects: |
R Medicine > R Medicine (General) > R856 Biomedical engineering. Electronics. Instrumentation. > R857.T55 Tissue engineering R Medicine > RD Surgery > RD93 Wounds and injuries Q Science > QP Physiology > QP501 Animal biochemistry > QP552.C6 Collagen |
| Creators: | Duan, Yonggang |
| Department: | School of Applied Sciences (to 2009) > Theses (to 2009) |
| Faculties, Divisions and Institutes: |
University Faculties, Divisions and Research Centres - OLD > Faculty of Arts, Science & Technology > Theses (Arts, Science & Technology) University Faculties, Divisions and Research Centres - OLD > School of Applied Sciences (to 2009) > Theses (to 2009) |
| Date: | 2007 |
| Date Type: | Completion |
| Language: | English |
| Status: | Unpublished |
| Institution: | The University of Northampton |
| URI: | http://nectar.northampton.ac.uk/id/eprint/2989 |
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