2018
DOI: 10.1080/05704928.2018.1426595
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FTIR analysis of natural and synthetic collagen

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Cited by 423 publications
(239 citation statements)
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“…Several characteristic peaks of PCL were found at 2920 cm –1 for asymmetric CH 2 stretching, 2865 cm –1 for symmetric CH 2 stretching, 1720 cm –1 for ester carbonyl group, 1290 cm –1 for CO and CC stretching, 1240 cm –1 for asymmetric COC stretching, and 1170 cm –1 for symmetric CO stretching; similar results were obtained by another researcher as well . For collagen, some typical bands were detected around 3300 cm –1 for amide A (NH stretching vibration), 1650 cm –1 for CNH 2 , 1530 cm –1 for CNH and 1240 cm –1 for CN (plane bending of NH and CN stretching vibration) . Regarding the chitosan, the spectrum showed 2 certain features at 1650 and 1600 cm –1 which are attributed to CNH 2 and CN of C=O stretching vibration and NH bending of NH 2 .…”
Section: Resultssupporting
confidence: 86%
“…Several characteristic peaks of PCL were found at 2920 cm –1 for asymmetric CH 2 stretching, 2865 cm –1 for symmetric CH 2 stretching, 1720 cm –1 for ester carbonyl group, 1290 cm –1 for CO and CC stretching, 1240 cm –1 for asymmetric COC stretching, and 1170 cm –1 for symmetric CO stretching; similar results were obtained by another researcher as well . For collagen, some typical bands were detected around 3300 cm –1 for amide A (NH stretching vibration), 1650 cm –1 for CNH 2 , 1530 cm –1 for CNH and 1240 cm –1 for CN (plane bending of NH and CN stretching vibration) . Regarding the chitosan, the spectrum showed 2 certain features at 1650 and 1600 cm –1 which are attributed to CNH 2 and CN of C=O stretching vibration and NH bending of NH 2 .…”
Section: Resultssupporting
confidence: 86%
“…Finally, Amide III showed a peak frequency of 1,238 cm −1 in R. Pulmo, compared to 1,240 cm −1 from human placenta and 1,243 cm −1 from rat tail tendon. The absorption intensity of 1,550 cm −1 (amide II) indicated that hydrogen bonding is present (Riaz et al, 2018); while absorption intensity of 1,238 cm-1 (amide III) confirmed that triple helical structure is intact (Riaz et al, 2018). FTIR confirmed the triple helix structure, high extent of intermolecular structure, and similar secondary structure of the proteins between different sources of collagen (Riaz et al, 2018).…”
Section: Fourier-transform Infrared (Atr-ftir) Spectroscopymentioning
confidence: 88%
“…FTIR generates a spectral fingerprint that can provide structural insights into collagen structure based on the presence and intensity of distinct peaks that correspond to amide A/B and amide I, II, and II bonds crucial to the formation of the triple helix (Belbachir et al, 2009;Riaz et al, 2018). The main absorption bands in R. pulmo collagen were amide A (3,283 cm −1 ), amide B (2,934 cm −1 ), amide I (1,647 cm −1 ), amide II (1,550 cm −1 ), and amide III (1,238 cm −1 ), typical bands for collagen type I (Figure 2).…”
Section: Fourier-transform Infrared (Atr-ftir) Spectroscopymentioning
confidence: 99%
“…This study presents new collagen-based materials for biomedical applications, especially in dentistry. These new materials, collagen-based spongy materials, obtained by the lyophilization method, were characterized by various techniques like optical microscopy, IR spectroscopy, water [30,31] Hydrogen bond between N-H stretch (ν NH ) and C-O (ν CO ) [29] 1607 1606 1608 1610…”
Section: Resultsmentioning
confidence: 99%