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Chemical crosslinking improves mechanical strength and stability in collagen-based scaffolds, highlighting the importance of cytocompatibility.
Collagen, as the predominant structural protein in vertebrates, represents a promising biomimetic material for scaffold development. Fibre-based scaffolds produced through textile technologies enable precise modulation of structural characteristics to closely mimic the extracellular matrix architecture using wet-spun collagen fibres. However, this in vitro fibre formation lacks natural crosslinking, resulting in collagen fibres with compromised mechanical strength, enzymatic resistance, and thermal stability compared to their native counterparts, thus restricting their biomedical applicability. Post-fabrication crosslinking is therefore imperative to enhance the durability and functional performance of collagen fibre-based scaffolds. Although traditional crosslinkers like glutaraldehyde effectively improve mechanical strength and stability, their clinical utility is hindered by cytotoxicity and associated adverse biological responses. Alternative synthetic crosslinking agents, such as hexamethylene diisocyanate, 1-Ethyl-3-(3’-dimethyl amino propyl) carbodiimide, and 1,4-Butanediol diglycidyl ether, have demonstrated superior cytocompatibility while effectively improving collagen fibre properties. Nonetheless, synthetic compounds may induce more pronounced foreign body reaction than natural agents, necessitating further investigation into their cytocompatibility across varying concentrations. In contrast, plant-based crosslinking offers a promising, cytocompatible alternative, significantly enhancing the thermal and mechanical stability of collagen fibres, provided that potential fibre discolouration is acceptable for intended biomedical applications.
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Schyra et al. (2025) studied this question.
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