Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/199782
Type: Artigo de periódico
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 1655 cm⁻¹/1690 cm⁻¹ absorbance ratio. The amide I area and the 1655 cm⁻¹/1690 cm⁻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: Amides
Animals
Anisotropy
Cattle
Collagen Type I
Microscopy, Polarization
Rats
Spectroscopy, Fourier Transform Infrared
Rights: fechado
Identifier DOI: 10.1016/j.micron.2010.09.010
Address: http://www.ncbi.nlm.nih.gov/pubmed/21134761
Date Issue: 2011
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

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