Journal
MICRON
Volume 42, Issue 3, Pages 283-289Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.micron.2010.09.010
Keywords
Amide I band; Birefringence; Collagen type I; FT-IR; Tendons
Categories
Funding
- Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP) [2003/04597-0, 2007/058251-8]
- Brazilian Council for Research and Development (CNPq)
- Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP) [03/04597-0] Funding Source: FAPESP
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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.
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