Affiliation:
1. Department of Biomaterials University of Bayreuth Prof.‐Rüdiger‐Bormann Str. 1 95447 Bayreuth Germany
2. Bayreuther Zentrum für Kolloide und Grenzflächen (BZKG) Bayreuther Zentrum für Molekulare Biowissenschaften (BZMB) Bayreuther Materialzentrum (BayMAT) Bayerisches Polymerinstitut (BPI) University of Bayreuth Universitätsstraße 30 95447 Bayreuth Germany
3. Faculty of Medicine University of Würzburg Pleicherwall 2 97070 Würzburg Germany
Abstract
AbstractCollagen 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.
Funder
Deutsche Forschungsgemeinschaft