on the publication serverTitle data
Mülller-Herrmann, Susanne ; Scheibel, Thomas:
Enzymatic Degradation of Films, Particles, and Nonwoven Meshes
Made of a Recombinant Spider Silk Protein.
In: ACS Biomaterials Science & Engineering.
Vol. 1
(March 2015)
Issue 4
.
- pp. 247-259.
ISSN 2373-9878
DOI: https://doi.org/10.1021/ab500147u
Abstract in another language
The performance of biomaterials in vivo is largely influenced by their stability and the rate and extent to which they degrade. Materials for tissue engineering applications, for example, have to be mechanically stable to support cell adhesion and proliferation without collapsing. On the other hand they need to be replaced gradually by native extracellular matrix and have to be (slowly) biodegradable. Therefore, it is of critical importance to be able to tune the degradation behavior of a biomaterial. Recombinantly produced spider silk proteins have been shown to be versatile biopolymers for medical applications. They can be processed into a variety of morphologies, and by chemical or genetic modification the properties can be adjusted to specific demands. Furthermore, in vivo experiments confirmed the lack of immunological reactions toward certain spider silks. In this study the degradation behavior of the recombinant spider silk protein eADF4(C16) in solution as well as processed into particles, films and nonwoven meshes was analyzed, and the impact of cross-linking of the scaffolds was assessed thereon. In addition to two bacterial proteolytic model enzymes, protease type XIV from Streptomyces griseus (PXIV) and collagenase type IA from Clostridium histolyticum (CHC) used in all experiments, several recombinant human matrix metalloproteinases (MMPs) and one elastase were used in studying degradation of soluble eADF4(C16). For soluble eADF4(C16) all degradation kinetics were similar. In case of eADF4(C16) scaffolds significant differences were observable between PXIV and CHC. All scaffolds were more stable toward proteolytic degradation in the presence of CHC than in the presence of PXIV. Further, particles were degraded significantly faster than films, and nonwoven meshes showed the highest proteolytic stability. Chemical cross-linking of the scaffolds led to a decrease in both degradation rate and extent.
Further data
| Item Type: | Article in a journal |
|---|---|
| Refereed: | Yes |
| Institutions of the University: | Faculties Faculties > Faculty of Engineering Science Faculties > Faculty of Engineering Science > Chair Biomaterials Faculties > Faculty of Engineering Science > Chair Biomaterials > Chair Biomaterials - Univ.-Prof. Dr. Thomas Scheibel Profile Fields > Advanced Fields > Advanced Materials Profile Fields > Advanced Fields > Molecular Biosciences Profile Fields > Advanced Fields > Polymer and Colloid Science Profile Fields > Emerging Fields > Food and Health Sciences Profile Fields Profile Fields > Advanced Fields Profile Fields > Emerging Fields |
| Result of work at the UBT: | Yes |
| DDC Subjects: | 600 Technology, medicine, applied sciences 600 Technology, medicine, applied sciences > 620 Engineering |
| Date Deposited: | 21 Sep 2015 12:30 |
| Last Modified: | 20 May 2016 07:31 |
| URI: | https://eref.uni-bayreuth.de/id/eprint/19464 |
