1. The process of EDC-NHS Cross-linking of reconstituted collagen fibres increases collagen fibrillar order and alignment
- Author
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Jennifer H. Shepherd, David V. Shepherd, Serena M. Best, S.J. Kew, Ruth E. Cameron, Siddhartha Ghose, Cameron, Ruth [0000-0003-1573-4923], Best, Serena [0000-0001-7866-8607], and Apollo - University of Cambridge Repository
- Subjects
0306 Physical Chemistry (incl. Structural) ,Atomic force microscopy ,Chemistry ,lcsh:Biotechnology ,General Engineering ,Polyethylene glycol ,macromolecular substances ,lcsh:QC1-999 ,Buffer (optical fiber) ,Article ,chemistry.chemical_compound ,symbols.namesake ,Chemical engineering ,Collagen fibres ,lcsh:TP248.13-248.65 ,Amide ,symbols ,Organic chemistry ,General Materials Science ,Extrusion ,Raman spectroscopy ,lcsh:Physics ,Carbodiimide - 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.
- Published
- 2014