and Characterization of Cytocompatibility and Biocompatibility of a Cross-linked Fish Collagen Wound Membrane.

Background/aim: The aim of the present research is a comprehensive evaluation of a fish-collagen based wound membrane using established and methodologies. A porcine pericardium membrane served as control material.

Materials And Methods: Scanning electron microscopy (SEM) and attenuated total reflection-Fourier transform infrared spectroscopy (ATR-FTIR) analysis were initially used to analyze the structure and collagen molecular structure. Also, a comparison of protein adsorption measurement of human serum albumin (HSA) adsorption was conducted. The membrane influence on cell viability, cell proliferation as well as their cytotoxic potential were examined . Additionally, the membrane tissue integration, degradation behavior and biocompatibility were investigated using the subcutaneous implantation model.

Results: The SEM analysis showed differences in the structure and the porosity of both membranes. The analysis FTIR spectroscopy revealed that collagen molecules are present in both membranes in their triple helical structure. The adsorption measurements showed that the surface density of HSA adsorbed to the fish collagen membrane surfaces was significantly lower compared to the values measured for the bovine pericardium membrane. Furthermore, both membranes demonstrated sufficient cytocompatibility in the indirect colorimetric XTT, LDH and BrdU assays. The study part revealed that the fish collagen membrane induced a faster biodegradation and a more pronounced pro-inflammatory tissue response, whereas the bovine pericardium membrane degrades more slowly.

Conclusion: The results of this study highlight the potential of fish collagen membranes as biocompatible wound healing materials. However, their rapid degradation presents a challenge that needs to be addressed through targeted modifications, such as optimized cross-linking.