Affiliation: | 1. Helmholtz Institute for Biomedical Engineering, BioInterface Group, RWTH Aachen University, Pauwelsstrasse 20, 52074 Aachen, Germany;2. Helmholtz Institute for Biomedical Engineering, BioInterface Group, RWTH Aachen University, Pauwelsstrasse 20, 52074 Aachen, Germany Interdisciplinary Centre for Clinical Research, RWTH Aachen University, Pauwelsstrasse 30, 52074 Aachen, Germany;3. Institute for Technical and Macromolecular Chemistry, RWTH Aachen University, Worringerweg 1, 52074 Aachen, Germany DWI – Leibniz Institute for Interactive Materials, RWTH Aachen University, Forckenbeckstraße 50, 52074 Aachen, Germany Aachen Maastricht Institute for Biobased Materials (AMIBM), Maastricht University, Brightlands Chemelot Campus, Urmonderbaan 22, Geleen, 6167 RD The Netherlands;4. Helmholtz Institute for Biomedical Engineering, BioInterface Group, RWTH Aachen University, Pauwelsstrasse 20, 52074 Aachen, Germany Department of Orthodontics, University Hospital RWTH Aachen, 52074 Aachen, Germany;5. Electron Microscopy Facility, Institute of Pathology, RWTH Aachen University, Pauwelsstrasse 30, 52074 Aachen, Germany |
Abstract: | Fibrin-based hydrogels are used as scaffolds in tissue engineering and regenerative medicine due to their biocompatibility, low cell toxicity, autologous production, and relevance for wound healing and clot formation. The availability of fibrinogen as well as its unique mechanical behavior exhibiting nonlinear elasticity makes it suitable for the fabrication of hydrogels. However, the broad application of fibrin hydrogels in biomaterials still faces challenges in terms of gel shrinkage and degradation processes. This can be addressed through the modulation of the hydrogels'r chemical and mechanical properties. In the present work, it is demonstrated that fibrin-based hydrogels with adjustable mechanical properties and controllable degradation profiles can be fabricated through the addition of fibrin-binding peptides. The cyclic peptide X2CXYYGTCLX (Tn7) is used, binding to fibrin by noncovalent supramolecular interactions. These new hydrogels exhibit no toxicity and reduced degradation rate at the same time supporting cell proliferation. Tn7 peptides significantly increase the Young's Modulus and mechanical stiffness as well as fibrin fiber thickness and inter-fiber crosslinking in hydrogels. In conclusion, hydrogels with optimized mechanical properties and controllable degradation profiles that can be advantageous for further approaches in tissue regeneration, cell-based therapies, or clinical treatment options are produced. |