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Title: The process of EDC-NHS cross-linking of reconstituted collagen fibres increases collagen fibrillar order and alignment

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 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.

Authors:
; ; ;  [1]; ;  [2]
  1. Department of Materials Science and Metallurgy, University of Cambridge, Cambridge (United Kingdom)
  2. Tigenix Ltd., Byron House, Cambridge Business Park, Cambridge (United Kingdom)
Publication Date:
OSTI Identifier:
22415237
Resource Type:
Journal Article
Resource Relation:
Journal Name: APL materials; Journal Volume: 3; Journal Issue: 1; Other Information: (c) 2014 Author(s); Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
36 MATERIALS SCIENCE; ATOMIC FORCE MICROSCOPY; COLLAGEN; COMPARATIVE EVALUATIONS; CROSS-LINKING; EXTRUSION; FIBERS; POLYETHYLENE GLYCOLS; RAMAN SPECTRA; RAMAN SPECTROSCOPY; WATER

Citation Formats

Shepherd, D. V., E-mail: dvs23@cam.ac.uk, Shepherd, J. H., Cameron, R. E., Best, S. M., Ghose, S., and Kew, S. J. The process of EDC-NHS cross-linking of reconstituted collagen fibres increases collagen fibrillar order and alignment. United States: N. p., 2015. Web. doi:10.1063/1.4900887.
Shepherd, D. V., E-mail: dvs23@cam.ac.uk, Shepherd, J. H., Cameron, R. E., Best, S. M., Ghose, S., & Kew, S. J. The process of EDC-NHS cross-linking of reconstituted collagen fibres increases collagen fibrillar order and alignment. United States. doi:10.1063/1.4900887.
Shepherd, D. V., E-mail: dvs23@cam.ac.uk, Shepherd, J. H., Cameron, R. E., Best, S. M., Ghose, S., and Kew, S. J. Thu . "The process of EDC-NHS cross-linking of reconstituted collagen fibres increases collagen fibrillar order and alignment". United States. doi:10.1063/1.4900887.
@article{osti_22415237,
title = {The process of EDC-NHS cross-linking of reconstituted collagen fibres increases collagen fibrillar order and alignment},
author = {Shepherd, D. V., E-mail: dvs23@cam.ac.uk and Shepherd, J. H. and Cameron, R. E. and Best, S. M. and Ghose, S. and Kew, S. J.},
abstractNote = {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 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.},
doi = {10.1063/1.4900887},
journal = {APL materials},
number = 1,
volume = 3,
place = {United States},
year = {Thu Jan 01 00:00:00 EST 2015},
month = {Thu Jan 01 00:00:00 EST 2015}
}