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Tissue Engineering

Tissue Engineering - Poster Session D

Poster BB13 - A comparative study of the effects of different crosslinking methods on the physicochemical properties of collagen multifilament bundles

Friday, October 25, 2024
3:30 PM - 4:30 PM EST
Location: Exhibit Hall E, F & G

Introduction:  Collagen-based scaffolds are promising materials for tissue engineering. Crosslinking is usually required to improve the mechanical properties and stability of collagen-based scaffolds. Introducing exogenous crosslinking into collagen may however affect the collagen structure. Since the architecture of collagen affects its functionality, it is important to study the effect of crosslinking methods to choose an ideal crosslinking method and condition to preserve the collagen structure and achieve the desired properties for tissue engineering applications. This study compares different chemical and physical crosslinking techniques on contact-drawn collagen multifilament bundles as a collagen-based scaffold model to recapitulate the structure of a tendon.

Materials and

Methods:  We investigated the range of conditions for different crosslinking methods to tune and improve the physicochemical properties of collagen-based scaffold without disturbing the collagen molecular structure for the desired tissue. We examine both physical (ultraviolet light, UVC) and chemical (genipin, carbodiimide (EDC), and glutaraldehyde) crosslinking methods. The presence of collagen and the formation of well-ordered collagen structures were confirmed by attenuated total reflectance Fourier-transform infrared spectromicroscopy (AT-FTIR) and X-ray diffraction (WAXS).

Results, Conclusions, and Discussions: The morphology of the collagen multifilament bundles was similar across crosslinking methods. Swelling of the multifilament bundles was dramatically reduced following crosslinking and varies by crosslinking method, with genipin- and carbodiimide-crosslinked specimens swelling the least. Ultimate tensile strength (UTS) and Young’s modulus significantly improved for all crosslinked specimens compared to non-crosslinked specimens, and it was possible to tune the mechanical properties of the tendon-like multifilament structures within the range of native tendons without interfering with collagen molecule architecture.

Acknowledgements (Optional):