Details
| Original language | English |
|---|---|
| Pages (from-to) | 95-102 |
| Number of pages | 8 |
| Journal | Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy |
| Volume | 214 |
| Early online date | 5 Feb 2019 |
| Publication status | Published - 5 May 2019 |
Abstract
Decellularized heart valves hold promise for their use as bioscaffolds in cardiovascular surgery. Quality assessment of heart valves after decellularization processing and/or storage is time consuming and destructive. Fourier transform infrared spectroscopy (FTIR) allows rapid non-invasive assessment of biomolecular structures in tissues. In this study, IR-spectra taken from different layers of the pulmonary artery trunk and leaflet tissues of decellularized porcine heart valves were compared with those of pure collagen and elastin, the main protein components in these tissues. In addition, spectral changes associated with aging and oxidative damage were investigated. Infrared absorbance spectra of the arteria intima and media layer were found to be very similar, whereas distinct differences were observed when compared with spectra of the externa layer. In the latter, the shape of the CH-stretching vibration region (3050–2800 cm −1 ) resembled that of pure collagen. Also, pronounced νCOOH and amide-II bands and a relatively high content of α-helical structures in the externa layer indicated the presence of collagen in this layer. The externa layer of the artery appeared to be sensitive to collagenase treatment, whereas the media and intima layer were particularly affected by elastase and not by collagenase treatment. Protein conformational changes after treatment with collagenase were observed in all three layers. Collagenase treatment completely degraded the leaflet tissue sections. Spectra were also collected from scaffolds after 2 and 12 weeks storage at 37 °C, and after induced oxidative damage. Spectral changes related to aging and oxidative damage were particularly evident in the CH-stretching region, whereas the shape of the amide-I band, reflecting the overall protein secondary structure, remained unaltered.
Keywords
- Biological scaffolds, Decellularization, FTIR, Oxidative damage, Pulmonary heart valve conduits, Spectral fingerprinting
ASJC Scopus subject areas
- Chemistry(all)
- Analytical Chemistry
- Physics and Astronomy(all)
- Atomic and Molecular Physics, and Optics
- Physics and Astronomy(all)
- Instrumentation
- Chemistry(all)
- Spectroscopy
Cite this
- Standard
- Harvard
- Apa
- Vancouver
- BibTeX
- RIS
In: Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy, Vol. 214, 05.05.2019, p. 95-102.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Spectral fingerprinting of decellularized heart valve scaffolds
AU - Vásquez-Rivera, Andrés
AU - Oldenhof, Harriëtte
AU - Hilfiker, Andres
AU - Wolkers, Willem F.
N1 - Funding Information: This research was supported by the German Research Foundation (DFG: Deutsche Forschungsgemeinschaft) via the Cluster of Excellence ‘From regenerative biology to reconstructive therapy’ (REBIRTH, EXC 62/1).
PY - 2019/5/5
Y1 - 2019/5/5
N2 - Decellularized heart valves hold promise for their use as bioscaffolds in cardiovascular surgery. Quality assessment of heart valves after decellularization processing and/or storage is time consuming and destructive. Fourier transform infrared spectroscopy (FTIR) allows rapid non-invasive assessment of biomolecular structures in tissues. In this study, IR-spectra taken from different layers of the pulmonary artery trunk and leaflet tissues of decellularized porcine heart valves were compared with those of pure collagen and elastin, the main protein components in these tissues. In addition, spectral changes associated with aging and oxidative damage were investigated. Infrared absorbance spectra of the arteria intima and media layer were found to be very similar, whereas distinct differences were observed when compared with spectra of the externa layer. In the latter, the shape of the CH-stretching vibration region (3050–2800 cm −1 ) resembled that of pure collagen. Also, pronounced νCOOH and amide-II bands and a relatively high content of α-helical structures in the externa layer indicated the presence of collagen in this layer. The externa layer of the artery appeared to be sensitive to collagenase treatment, whereas the media and intima layer were particularly affected by elastase and not by collagenase treatment. Protein conformational changes after treatment with collagenase were observed in all three layers. Collagenase treatment completely degraded the leaflet tissue sections. Spectra were also collected from scaffolds after 2 and 12 weeks storage at 37 °C, and after induced oxidative damage. Spectral changes related to aging and oxidative damage were particularly evident in the CH-stretching region, whereas the shape of the amide-I band, reflecting the overall protein secondary structure, remained unaltered.
AB - Decellularized heart valves hold promise for their use as bioscaffolds in cardiovascular surgery. Quality assessment of heart valves after decellularization processing and/or storage is time consuming and destructive. Fourier transform infrared spectroscopy (FTIR) allows rapid non-invasive assessment of biomolecular structures in tissues. In this study, IR-spectra taken from different layers of the pulmonary artery trunk and leaflet tissues of decellularized porcine heart valves were compared with those of pure collagen and elastin, the main protein components in these tissues. In addition, spectral changes associated with aging and oxidative damage were investigated. Infrared absorbance spectra of the arteria intima and media layer were found to be very similar, whereas distinct differences were observed when compared with spectra of the externa layer. In the latter, the shape of the CH-stretching vibration region (3050–2800 cm −1 ) resembled that of pure collagen. Also, pronounced νCOOH and amide-II bands and a relatively high content of α-helical structures in the externa layer indicated the presence of collagen in this layer. The externa layer of the artery appeared to be sensitive to collagenase treatment, whereas the media and intima layer were particularly affected by elastase and not by collagenase treatment. Protein conformational changes after treatment with collagenase were observed in all three layers. Collagenase treatment completely degraded the leaflet tissue sections. Spectra were also collected from scaffolds after 2 and 12 weeks storage at 37 °C, and after induced oxidative damage. Spectral changes related to aging and oxidative damage were particularly evident in the CH-stretching region, whereas the shape of the amide-I band, reflecting the overall protein secondary structure, remained unaltered.
KW - Biological scaffolds
KW - Decellularization
KW - FTIR
KW - Oxidative damage
KW - Pulmonary heart valve conduits
KW - Spectral fingerprinting
UR - http://www.scopus.com/inward/record.url?scp=85061317123&partnerID=8YFLogxK
U2 - 10.1016/j.saa.2019.02.006
DO - 10.1016/j.saa.2019.02.006
M3 - Article
C2 - 30769156
AN - SCOPUS:85061317123
VL - 214
SP - 95
EP - 102
JO - Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy
JF - Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy
SN - 1386-1425
ER -