dc.creatorDe Campos Vidal B.
dc.creatorMello M.L.S.
dc.date2011
dc.date2015-06-30T20:41:58Z
dc.date2015-11-26T14:53:51Z
dc.date2015-06-30T20:41:58Z
dc.date2015-11-26T14:53:51Z
dc.date.accessioned2018-03-28T22:05:42Z
dc.date.available2018-03-28T22:05:42Z
dc.identifier
dc.identifierMicron. , v. 42, n. 3, p. 283 - 289, 2011.
dc.identifier9684328
dc.identifier10.1016/j.micron.2010.09.010
dc.identifierhttp://www.scopus.com/inward/record.url?eid=2-s2.0-78650755968&partnerID=40&md5=07bb6335eb8bb39c934c6bcb53b79e5c
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/108929
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/108929
dc.identifier2-s2.0-78650755968
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1255021
dc.descriptionCollagen 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.
dc.description42
dc.description3
dc.description283
dc.description289
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dc.languageen
dc.publisher
dc.relationMicron
dc.rightsfechado
dc.sourceScopus
dc.titleCollagen Type I Amide I Band Infrared Spectroscopy
dc.typeArtículos de revistas


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