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(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.)

Collagen type I amide I band infrared spectroscopy

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Autor(es):
Vidal, Benedicto de Campos [1] ; Mello, Maria Luiza S. [1]
Número total de Autores: 2
Afiliação do(s) autor(es):
[1] Univ Campinas UNICAMP, Inst Biol, Dept Anat Cell Biol & Physiol & Biophys, BR-13083863 Campinas, SP - Brazil
Número total de Afiliações: 1
Tipo de documento: Artigo de Revisão
Fonte: Micron; v. 42, n. 3, p. 283-289, APR 2011.
Citações Web of Science: 124
Resumo

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. (C) 2010 Elsevier Ltd. All rights reserved. (AU)

Processo FAPESP: 03/04597-0 - Ordem molecular e organização supramolecular em feixes de colágeno: diferenças com a funcionalidade, como suposto efeito de expressão de patogenia, e contribuição metodológica
Beneficiário:Benedicto de Campos Vidal
Modalidade de apoio: Auxílio à Pesquisa - Regular