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URN to cite this document: urn:nbn:de:bvb:703-epub-8422-6
Title data
Koeck, Kim Sarah ; Trossmann, Vanessa T. ; Scheibel, Thomas:
3D-Printed and Recombinant Spider Silk Particle Reinforced Collagen Composite Scaffolds for Soft Tissue Engineering.
In: Advanced Functional Materials.
Vol. 35
(2025)
Issue 15
.
- 2407760.
ISSN 1616-3028
DOI der Verlagsversion: https://doi.org/10.1002/adfm.202407760
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Project information
| Project title: |
Project's official title Project's id TRR 225 Biofabrication 326998133 |
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| Project financing: |
Deutsche Forschungsgemeinschaft |
Abstract
Collagen is one main component of the extracellular matrix (ECM) in natural tissues and is, therefore, well suited as a biomaterial for tissue engineering. In this study, a method is presented to 3D-bioprint collagen into a precipitation bath comprising recombinantly produced spider silk protein eADF4(C16) yielding a composite with excellent mechanical properties. The spider silk precipitation bath induced assembly of the collagen into fibrils, and subsequent addition of potassium phosphate buffer lead to the formation of silk particles and stabilization of the collagen fibrils. The produced collagen-silk composite scaffolds show an internal structure of homogeneously distributed and interacting collagen fibrils and spider silk particles with significantly better mechanical properties compared to plain collagen scaffolds. Further, enzymatic degradation assays of the scaffolds over a 7-day period show higher stability of the collagen-silk scaffolds compared to plain collagen scaffolds in the presence of wound proteases. Using the spider silk variant eADF4(C16-RGD) further increases compressive stress and elastic modulus compared to that of the unmodified variant. Finally, it is shown that the unique collagen-spider silk composite scaffolds comprising the cell-binding domains of collagen and the RGD sequence in the spider silk variant represent a promising material for soft tissue regeneration.
Further data
| Item Type: | Article in a journal |
|---|---|
| Keywords: | collagen-silk-composites; nanofibrils; protein–protein-interactions; self-assembly |
| DDC Subjects: | 600 Technology, medicine, applied sciences > 620 Engineering |
| Institutions of the University: | Faculties > Faculty of Engineering Science > Chair Biomaterials > Chair Biomaterials - Univ.-Prof. Dr. Thomas Scheibel Faculties Faculties > Faculty of Engineering Science Faculties > Faculty of Engineering Science > Chair Biomaterials |
| Language: | English |
| Originates at UBT: | Yes |
| URN: | urn:nbn:de:bvb:703-epub-8422-6 |
| Date Deposited: | 22 Apr 2025 07:03 |
| Last Modified: | 22 Apr 2025 07:03 |
| URI: | https://epub.uni-bayreuth.de/id/eprint/8422 |
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