Abstract
We describe the production of collagen fibre bundles through a multi-strand, semi-continuous extrusion process. Cross-linking using an EDC (1-ethyl-3-(3-dimethylaminopropyl)carbodiimide), NHS (N-hydroxysuccinimide) combination was considered. Atomic Force Microscopy (AFM) and Raman spectroscopy focused on how cross-linking affected the collagen fibrillar structure. In the cross-linked fibres, a clear fibrillar structure comparable to native collagen was observed which was not observed in the non-cross-linked fibre. The amide III doublet in the Raman spectra provided additional evidence of alignment in the cross-linked fibres. Raman spectroscopy also indicated no residual polyethylene glycol (from the fibre forming buffer) or water in any of the fibres.
Highlights
We describe the production of collagen fibre bundles through a multi-strand, semicontinuous extrusion process
Atomic Force Microscopy and Raman spectroscopy focused on how crosslinking affected the collagen fibrillar structure
The authors have previously settled upon the use of the zero length cross-linker carbodiimide 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC) in combination with N-hydroxysuccinimide (NHS) as an effective route for the cross-linking of extruded collagen fibres.[11,12,13]
Summary
We describe the production of collagen fibre bundles through a multi-strand, semicontinuous extrusion process. The aim of the work was to study the effects of cross-linking of collagen fibres extruded through a semi-continuous process[13] using AFM and Raman spectroscopy.
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