Abstract
Collagen is the most abundant extracellular matrix (ECM) protein in the human body, thus widely used in tissue engineering and subsequent clinical applications. This study aimed to extract collagen from ovine (Ovis aries) Achilles tendon (OTC), and to evaluate its physicochemical properties and its potential to fabricate thin film with collagen fibrils in a random or aligned orientation. Acid-solubilized protein was extracted from ovine Achilles tendon using 0.35 M acetic acid, and 80% of extracted protein was measured as collagen. SDS-PAGE and mass spectrometry analysis revealed the presence of alpha 1 and alpha 2 chain of collagen type I (col I). Further analysis with Fourier transform infrared spectrometry (FTIR), X-ray diffraction (XRD) and energy dispersive X-ray spectroscopy (EDS) confirms the presence of triple helix structure of col I, similar to commercially available rat tail col I. Drying the OTC solution at 37°C resulted in formation of a thin film with randomly orientated collagen fibrils (random collagen film; RCF). Introduction of unidirectional mechanical intervention using a platform rocker prior to drying facilitated the fabrication of a film with aligned orientation of collagen fibril (aligned collagen film; ACF). It was shown that both RCF and ACF significantly enhanced human dermal fibroblast (HDF) attachment and proliferation than that on plastic surface. Moreover, cells were distributed randomly on RCF, but aligned with the direction of mechanical intervention on ACF. In conclusion, ovine tendon could be an alternative source of col I to fabricate scaffold for tissue engineering applications.
| Original language | English |
|---|---|
| Pages (from-to) | 163-171 |
| Number of pages | 9 |
| Journal | Materials Science and Engineering C |
| Volume | 68 |
| DOIs | |
| Publication status | Published - 1 Nov 2016 |
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Keywords
- Biocompatibility
- Cell alignment
- Collagen film
- Collagen type I
- Ovine collagen
- Tissue engineering
- Unidirectional alignment
ASJC Scopus subject areas
- Materials Science(all)
- Condensed Matter Physics
- Mechanical Engineering
- Mechanics of Materials
Cite this
Ovine tendon collagen : Extraction, characterisation and fabrication of thin films for tissue engineering applications. / Fauzi, M. B.; Lokanathan, Y.; Aminuddin, B. S.; Ruszymah, B. H I; Chowdhury, S. R.
In: Materials Science and Engineering C, Vol. 68, 01.11.2016, p. 163-171.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Ovine tendon collagen
T2 - Extraction, characterisation and fabrication of thin films for tissue engineering applications
AU - Fauzi, M. B.
AU - Lokanathan, Y.
AU - Aminuddin, B. S.
AU - Ruszymah, B. H I
AU - Chowdhury, S. R.
PY - 2016/11/1
Y1 - 2016/11/1
N2 - Collagen is the most abundant extracellular matrix (ECM) protein in the human body, thus widely used in tissue engineering and subsequent clinical applications. This study aimed to extract collagen from ovine (Ovis aries) Achilles tendon (OTC), and to evaluate its physicochemical properties and its potential to fabricate thin film with collagen fibrils in a random or aligned orientation. Acid-solubilized protein was extracted from ovine Achilles tendon using 0.35 M acetic acid, and 80% of extracted protein was measured as collagen. SDS-PAGE and mass spectrometry analysis revealed the presence of alpha 1 and alpha 2 chain of collagen type I (col I). Further analysis with Fourier transform infrared spectrometry (FTIR), X-ray diffraction (XRD) and energy dispersive X-ray spectroscopy (EDS) confirms the presence of triple helix structure of col I, similar to commercially available rat tail col I. Drying the OTC solution at 37°C resulted in formation of a thin film with randomly orientated collagen fibrils (random collagen film; RCF). Introduction of unidirectional mechanical intervention using a platform rocker prior to drying facilitated the fabrication of a film with aligned orientation of collagen fibril (aligned collagen film; ACF). It was shown that both RCF and ACF significantly enhanced human dermal fibroblast (HDF) attachment and proliferation than that on plastic surface. Moreover, cells were distributed randomly on RCF, but aligned with the direction of mechanical intervention on ACF. In conclusion, ovine tendon could be an alternative source of col I to fabricate scaffold for tissue engineering applications.
AB - Collagen is the most abundant extracellular matrix (ECM) protein in the human body, thus widely used in tissue engineering and subsequent clinical applications. This study aimed to extract collagen from ovine (Ovis aries) Achilles tendon (OTC), and to evaluate its physicochemical properties and its potential to fabricate thin film with collagen fibrils in a random or aligned orientation. Acid-solubilized protein was extracted from ovine Achilles tendon using 0.35 M acetic acid, and 80% of extracted protein was measured as collagen. SDS-PAGE and mass spectrometry analysis revealed the presence of alpha 1 and alpha 2 chain of collagen type I (col I). Further analysis with Fourier transform infrared spectrometry (FTIR), X-ray diffraction (XRD) and energy dispersive X-ray spectroscopy (EDS) confirms the presence of triple helix structure of col I, similar to commercially available rat tail col I. Drying the OTC solution at 37°C resulted in formation of a thin film with randomly orientated collagen fibrils (random collagen film; RCF). Introduction of unidirectional mechanical intervention using a platform rocker prior to drying facilitated the fabrication of a film with aligned orientation of collagen fibril (aligned collagen film; ACF). It was shown that both RCF and ACF significantly enhanced human dermal fibroblast (HDF) attachment and proliferation than that on plastic surface. Moreover, cells were distributed randomly on RCF, but aligned with the direction of mechanical intervention on ACF. In conclusion, ovine tendon could be an alternative source of col I to fabricate scaffold for tissue engineering applications.
KW - Biocompatibility
KW - Cell alignment
KW - Collagen film
KW - Collagen type I
KW - Ovine collagen
KW - Tissue engineering
KW - Unidirectional alignment
UR - http://www.scopus.com/inward/record.url?scp=84971641374&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84971641374&partnerID=8YFLogxK
U2 - 10.1016/j.msec.2016.05.109
DO - 10.1016/j.msec.2016.05.109
M3 - Article
C2 - 27524008
AN - SCOPUS:84971641374
VL - 68
SP - 163
EP - 171
JO - Materials Science and Engineering C
JF - Materials Science and Engineering C
SN - 0928-4931
ER -