Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/108929
Type: Artigo
Title: Collagen type I amide I band infrared spectroscopy
Author: Vidal, Benedicto de Campos
Mello, Maria Luiza S.
Abstract: Collagen fiber structure and organization have been found to vary in different tendon types. Differences have been reported in the FT-IR spectra of the amide I band of collagen-containing structures. In the present study, the FT-IR spectral characteristics of the amide I band of the bovine flexor tendon and the extended rat tail tendon were compared by using the diamond attenuated total reflectance technique. The objective was to associate FT-IR spectral characteristics in tendons with their different collagen fiber supraorganization and biomechanical properties. Nylon 6 and poly-l-lysine were used as polyamide models. Each of these materials was found to exhibit molecular order and crystallinity, as revealed by their birefringence. The following FT-IR parameters were evaluated: amide I band profile, absorption peaks and areas, and the 1655cm -1/1690cm -1 absorbance ratio. The amide I area and the 1655cm -1/1690cm -1 absorbance ratio were significantly higher for the bovine flexor tendon, indicating that its collagen fibers are richer in pyridinoline-type cross-linking, proline and/or hydroxyproline and H-bonding, and that these fibers are more packed and supraorganizationally ordered than those in the rat tail tendon. This conclusion is additionally supported by differences in collagen solubility and biochemical/biomechanical properties of the tendons. © 2010 Elsevier Ltd.
Collagen fiber structure and organization have been found to vary in different tendon types. Differences have been reported in the FT-IR spectra of the amide I band of collagen-containing structures. In the present study, the FT-IR spectral characteristics of the amide I band of the bovine flexor tendon and the extended rat tail tendon were compared by using the diamond attenuated total reflectance technique. The objective was to associate FT-IR spectral characteristics in tendons with their different collagen fiber supraorganization and biomechanical properties. Nylon 6 and poly-l-lysine were used as polyamide models. Each of these materials was found to exhibit molecular order and crystallinity, as revealed by their birefringence. The following FT-IR parameters were evaluated: amide I band profile, absorption peaks and areas, and the 1655cm -1/1690cm -1 absorbance ratio. The amide I area and the 1655cm -1/1690cm -1 absorbance ratio were significantly higher for the bovine flexor tendon, indicating that its collagen fibers are richer in pyridinoline-type cross-linking, proline and/or hydroxyproline and H-bonding, and that these fibers are more packed and supraorganizationally ordered than those in the rat tail tendon. This conclusion is additionally supported by differences in collagen solubility and biochemical/biomechanical properties of the tendons.
Subject: Amidas
Birrefringência
Colágeno tipo I
Fourier, Espectroscopia de infravermelho por transformada de
Tendões
Espectro de absorção
Country: Estados Unidos
Editor: Pergamon Press
Citation: Micron. , v. 42, n. 3, p. 283 - 289, 2011.
Rights: fechado
Identifier DOI: 10.1016/j.micron.2010.09.010
Address: https://www-sciencedirect.ez88.periodicos.capes.gov.br/science/article/pii/S0968432810002623
Date Issue: 2011
Appears in Collections:IB - Artigos e Outros Documentos

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