Northampton Electronic Collection of Theses and Research

Factors influencing the properties of reconstituted collagen fibers prior to self-assembly: animal species and collagen extraction method

Zeugolis, D. I., Paul, R. G. and Attenburrow, G. E. (2008) Factors influencing the properties of reconstituted collagen fibers prior to self-assembly: animal species and collagen extraction method. Journal of Biomedical Materials Research Part A: Applied Biomaterials. 86A(4), pp. 892-904. 1549-3296.

Item Type: Article
Abstract: This research work allows a direct comparison between collagen solutions of equal concentration derived from the two widely used collagen sources: bovine Achilles tendon (BAT) and rat tail tendon (RTT), and extraction methods: acid (AS) and pepsin (PS) solubilization on the properties of extruded collagen fibers. Scanning electron microscopy revealed that the substructure of the collagen fibers was the same independent of the treatment. Transmission electron microscopy revealed that the AS collagen-derived fibers were comprised of thick quarter-staggered fibrils, while the coexistence of thin nonbanded and thick banded fibrils was apparent for the PS collagen-derived fibers. The BAT-derived fibers demonstrated higher denaturation temperature than the RTT-derived ones (p < 0.05). The extraction method had no influence on the thermal characteristics of the fibers produced (p > 0.05). ASBAT collagen was of higher viscosity than both ASRTT and PSBAT (p < 0.002), and therefore larger diameter fibers were obtained (p < 0.001). An inversely proportional relationship between dry-fiber diameter and stress at break was observed within the treatments. The PS yielded 10 times more soluble collagen from BAT and the derived fibers were of similar tensile strength, stiffness, and elongation (p > 0.05) as those derived from the AS collagen. No significant difference was observed for the stress at break for the ASBAT and the ASRTT, while significant difference was observed for the elongation and modulus values (p < 0.005). Overall, reconstituted collagen fibers were produced with properties similar to native or synthetic fibers to suit a wide range of tissue engineering applications
Uncontrolled Keywords: acid and pepsin soluble collagen, bovine Achilles tendon and rat tail tendon collagen, reconstituted collagen fibers, electron microscopy, mechanical and thermal properties
Subjects: R Medicine > R Medicine (General) > R856 Biomedical engineering. Electronics. Instrumentation.
T Technology > TP Chemical technology > TP248.13 Biotechnology
Q Science > QP Physiology > QP501 Animal biochemistry > QP552.C6 Collagen
Creators: Zeugolis, D I, Paul, R G and Attenburrow, Geoff E
Publisher: John Wiley & Sons
Faculties, Divisions and Institutes: University Faculties, Divisions and Research Centres - OLD > Research Centre > Centre for Research on Leather and Materials Science
Research Institutes > Institute for Creative Leather Technologies
Date: September 2008
Date Type: Publication
Page Range: pp. 892-904
Journal or Publication Title: Journal of Biomedical Materials Research Part A: Applied Biomaterials
Volume: 86A
Number: 4
Language: English
DOI: 10.1002/jbm.a.31694
ISSN: 1549-3296
Status: Published / Disseminated
Refereed: Yes
URI: http://nectar.northampton.ac.uk/id/eprint/1872

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