Corrigendum: Wet spinning and riboflavin crosslinking of collagen type I/III filaments (2019 Biomed. Mater. 14 015007)

Abstract

Reconstituted fibrillary collagen is one of the most advantageous biomaterials for biomedical applications. The objective of the research project described in this paper was to evaluate whether riboflavin-induced photo-crosslinking could be used as a non-toxic alternative to glutaraldehyde (GA)-crosslinking for the preparation of wet spun collagen filaments. Collagen filaments were produced on a laboratory wet spinning line and crosslinked with GA or riboflavin with and without UV exposure. Based on mechanical and thermal analyses, it was concluded that the combination of riboflavin and UV light leads to crosslinked collagen filaments having improved mechanical and thermal properties. Furthermore, riboflavin-crosslinked filaments exhibited a higher cytocompatibility for human mesenchymal stem cells compared to glutaraldehyde crosslinked filaments.

Hierarchically Assembled Type I Collagen Fibres as Biomimetic Building Blocks of Biomedical Membranes

“…DSC thermograms of the UV-cured CRT hydrogels indicated an endothermic transition at 86–96 °C, which is attributed to the denaturation of collagen triple helices into random coils [ 20 , 22 , 35 ]. Variations of sample 4VBC-MA concentration ( c = 0.4 → 0.8 wt.%) in respective hydrogel-forming solutions were found to directly impact on the T d (86 → 96 °C) of each resulting hydrogel ( Figure 3 A), in line with the concentration-induced effect on the crosslink density and thermal stabilisation of triple helices [ 20 , 22 , 23 ].…”

“…Recapitulation of aligned collagen fibrils via fibrillogenesis ex vivo enables mimicry of specific tissue architectures, e.g., aligned tendons [ 23 ], and to introduce an additional experimental dimension to tune the tensile properties of respective collagen material. Self-assembly of collagen triple helices into fibrils has been demonstrated in wet spun CRT samples via fibre incubation in aqueous buffer (37 °C, 24 h) [ 24 , 25 ].…”

“…Wet spinning has proven to be a particularly successful method to produce individual collagen fibres [ 21 ] and multifilament yarns [ 22 ] of collagen triple helices, enabling further generation of fibrous assemblies and three-dimensional macroscopic fabrics. At the same time, crosslinking of collagen post-spinning is still associated with issues with respect to the safety and macroscopic properties of the resulting products [ 23 ]. Indeed, current synthetic crosslinking methods are typically carried out in the wet state, generating risks of uncontrollable fibre swelling and alteration of fibre morphology during the crosslinking.…”