dc.creator | De Campos Vidal B. | |
dc.creator | Mello M.L.S. | |
dc.date | 2011 | |
dc.date | 2015-06-30T20:41:58Z | |
dc.date | 2015-11-26T14:53:51Z | |
dc.date | 2015-06-30T20:41:58Z | |
dc.date | 2015-11-26T14:53:51Z | |
dc.date.accessioned | 2018-03-28T22:05:42Z | |
dc.date.available | 2018-03-28T22:05:42Z | |
dc.identifier | | |
dc.identifier | Micron. , v. 42, n. 3, p. 283 - 289, 2011. | |
dc.identifier | 9684328 | |
dc.identifier | 10.1016/j.micron.2010.09.010 | |
dc.identifier | http://www.scopus.com/inward/record.url?eid=2-s2.0-78650755968&partnerID=40&md5=07bb6335eb8bb39c934c6bcb53b79e5c | |
dc.identifier | http://www.repositorio.unicamp.br/handle/REPOSIP/108929 | |
dc.identifier | http://repositorio.unicamp.br/jspui/handle/REPOSIP/108929 | |
dc.identifier | 2-s2.0-78650755968 | |
dc.identifier.uri | http://repositorioslatinoamericanos.uchile.cl/handle/2250/1255021 | |
dc.description | 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. | |
dc.description | 42 | |
dc.description | 3 | |
dc.description | 283 | |
dc.description | 289 | |
dc.description | Aparicio, S., Doty, S.B., Camacho, N.P., Pachalis, E.P., Spevak, L., Mendelsohn, R., Boskei, A.L., Optimal methods for processing mineralized tissues for Fourier transform infrared microspectroscopy (2002) Calcif. Tissue Int., 70, pp. 422-429 | |
dc.description | Benjamin, M., Kaiser, E., Milz, S., Structure-function relationships: a review (2008) J. Anat., 212, pp. 211-228 | |
dc.description | Bi, X., Li, G., Doty, S.B., Camacho, N.P., A novel method for determination of collagen orientation in cartilage by Fourier transform infrared imaging spectroscopy (FT-IRIS) (2005) Osteoarthr. Cartil., 13, pp. 1050-1058 | |
dc.description | Blank, R.D., Baldini, T.H., Kaufman, M., Bailey, S., Gupta, R., Yershov, Y., Boskey, A.L., Paschalis, E.P., Spectroscopically determined collagen Pyr/deH-DHLNL cross-link ratio and crystallinity indices differ markedly in recombinant congenic mice with divergent calculated bone tissue strength (2003) Connect. Tissue Res., 44, pp. 134-142 | |
dc.description | Boskey, A., Camacho, N.P., FT-IR imaging of native and tissue-engineered bone and cartilage (2007) Biomaterials, 28, pp. 2465-2478 | |
dc.description | Bryan, M.A., Brauner, J.W., Anderie, G., Flach, C.R., Brodsky, B., Mendelsohn, R., FTIR studies of collagen model peptides: complementary experimental and simulation approaches to conformation and unfolding (2007) J. Am. Chem. Soc., 129, pp. 7877-7884 | |
dc.description | Camacho, N.P., West, P., Torzilli, P.A., Mendelsohn, R., FTIR microscopic imaging of collagen and proteoglycan in bovine cartilage (2001) Biopolymers, 62, pp. 1-8 | |
dc.description | Coats, A.M., Hukins, D.W.L., Imrie, C.T., Aspden, R.M., Polarization artefacts of an FTIR microscope and the consequences for intensity measurements on anisotropic materials (2003) J. Microsc., 211, pp. 63-66 | |
dc.description | Fouda, I.M., Evaluation of the form birefringence and other structural parameters due to thermal annealing for nylon 6 fibers (2002) J. Polym. Res.-Taiwan, 9, pp. 37-44 | |
dc.description | Griffiths, P.R., Haseth, J.A., (2007) Fourier Transform Infrared Spectrometry, , Wiley-Interscience, Hoboken, USA | |
dc.description | Hamza, A.A., Fouda, I.M., El-Farahaty, K.A., Seisa, E.A., Optomechanical properties of fibres. 1. Optical anisotropy in stretched nylon-6 fibers (1991) Polymer Test., 10, pp. 83-90 | |
dc.description | Jackson, M., Mantsch, H.H., The use and misuse of FTIR spectroscopy in the determination of protein structure (1995) CRC Crit. Rev. Biochem. Mol. Biol., 30, pp. 95-120 | |
dc.description | Jastrzebska, M., Zalewska-Rejdak, J., Mróz, I., Barwinski, B.I., Wrzalik, R., Kocot, A., Nozynski, J., Atomic force microscopy and FT-IR spectroscopy investigations of human heart valves (2006) Gen. Physiol. Biophys., 25, pp. 231-244 | |
dc.description | Józsa, L.G., Kannus, P., (1997) Human Tendons Anatomy, Physiology, and Pathology, p. 573. , Human Kinetics, Champaign, USA | |
dc.description | Kaminska, A., Sionkowska, A., Effect of UV radiation on the infrared spectra of collagen (1996) Polymer Degrad. Stab., 51, pp. 19-26 | |
dc.description | Ker, R.F., Mechanics of tendon, from an engineering perspective (2007) Int. J. Fatigue, 29, pp. 1001-1009 | |
dc.description | Kjaer, M., Role of the extracellular matrix in adaptation of tendon and skeletal muscle to mechanical loading (2004) Physiol. Rev., 84, pp. 649-698 | |
dc.description | Lazarev, Y.A., Grishkovsky, B.A., Khromova, T.B., Amide I band of IR spectrum and structure of collagen and related polypeptides (1985) Biopolymers, 24, pp. 1449-1478 | |
dc.description | Lee, K.-H., Kim, K.-W., Pesapane, A., Kim, H.-Y., Rabolt, J.F., Polarized FT-IR study of macroscopically oriented electrospun nylon-6 nanofibers (2008) Macromolecules, 41, pp. 1494-1498 | |
dc.description | Liu, K.-Z., Jackson, M., Sowa, M.G., Ju, H., Dixon, I.M.C., Mantsch, H.H., Modification of the extracellular matrix following myocardial infarction monitored by FTIR spectroscopy (1996) Biochim. Biophys. Acta, 1315, pp. 73-77 | |
dc.description | Mello, M.L.S., Vidal, B.C., Experimental tendon repair: glycosaminoglycan arrangement in newly synthesized collagen fibers (2003) Cell Mol. Biol., 49, pp. 579-585 | |
dc.description | Nakagaki, W.R., Pimentel, E.R., Benevides, G.P., Gomes, L., The effect of age and spontaneous exercise on the biochemical and biophysical properties of chicken superficial digital flexor tendon (2010) Connect. Tissue Res., 51, pp. 265-273 | |
dc.description | Payne, K.J., Veis, A., Fourier transform IR spectroscopy of collagen and gelatin solutions: deconvolution of the amide I band for conformational studies (1988) Biopolymers, 27, pp. 1749-1760 | |
dc.description | Sellaro, T.L., Hildebrand, D., Lu, Q.J., Vyavahare, N., Scott, M., Sacks, M.S., Effects of collagen fiber orientation on the response of biologically derived soft tissue biomaterials to cyclic loading (2007) J. Biomed. Mater. Res., 80 A, pp. 194-205 | |
dc.description | Singh, B.R., (2000) Infrared Analysis of Peptides and Proteins: Principles and Applications. Amer. Chem. Soc. Series 750, p. 240. , Oxford Univ. Press, Corby, UK | |
dc.description | Susi, H., Ard, J.S., Carroll, R.J., The infrared spectrum and water binding of collagen as a function of relative humidity (1971) Biopolymers, 10, pp. 1597-1604 | |
dc.description | Tiong, W.H.C., Damodaran, G., Naik, H., Kelly, J.L., Pandit, A., Enhancing amine terminals in an amine-deprived collagen matrix (2008) Langmuir, 24, pp. 11752-11761 | |
dc.description | Twardowski, J., Anzenbacher, P., (1994) Raman and IR Spectroscopy in Biology and Biochemistry, , Ellis Horwood Ltd., Chichester, UK | |
dc.description | Vidal, B.C., The part played by mucopolysaccharides in the form birefringence of collagen (1965) Protoplasma, 59, pp. 472-479 | |
dc.description | Vidal, B.C., Evaluation of carbohydrate role in the molecular order of collagen bundles. Microphotometric measurements of textural birefringence (1986) Cell Mol. Biol., 32, pp. 527-531 | |
dc.description | Vidal, B.C., Crimp as part of a helical structure (1995) C. R. Acad. Sci. Paris Sci. Vie/Life Sci., 318, pp. 173-178 | |
dc.description | Vidal, B.C., From collagen type I solution to fibers with helical pattern: a self-assembly phenomenon (1995) C. R. Acad. Sci. Paris Sci. Vie/Life Sci., 318, pp. 831-836 | |
dc.description | Vidal, B.C., Image analysis of tendon superstructure using interference and polarized light microscopy (2003) Micron, 34, pp. 423-432 | |
dc.description | Vidal, B.C., Mello, M.L.S., Structural organization of collagen fibers in chordae tendinae as assessed by optical anisotropic properties and fast Fourier transform (2009) J. Struct. Biol., 167, pp. 166-175 | |
dc.description | Vidal, B.C., Mello, M.L.S., Optical anisotropy of collagen fibers of rat calcaneal tendons: an approach to spatially resolved supramolecular organization (2010) Acta Histochem., 112, pp. 53-61 | |
dc.description | Vigano, C., Manciu, L., Buyse, F., Goormaghtigh, E., Ruysschaert, J.-M., Attenuated total reflection IR spectroscopy as a tool to investigate the structure, orientation and tertiary structure changes in peptides and membrane proteins (2000) Biopolymers, 55, pp. 373-380 | |
dc.description | Viidik, A., Nieksen, H.M., Skalicky, M., Influence of physical exercise on aging rats: II. Life-long exercise delays aging of tail tendon collagen (1996) Mech. Age. Devel., 88, pp. 139-148 | |
dc.description | Vilarta, R., Vidal, B.D., Anisotropic and biomechanical properties of tendons modified by exercise and denervation-aggregation and macromolecular order in collagen bundles (1989) Matrix, 9, pp. 55-61 | |
dc.description | Wagnusson, S.P., Hansn, P., Kjaer, M., Tendon properties in relation to muscular activity and physical training (2003) J. Med. Sci. Sports, 13, pp. 211-223 | |
dc.language | en | |
dc.publisher | | |
dc.relation | Micron | |
dc.rights | fechado | |
dc.source | Scopus | |
dc.title | Collagen Type I Amide I Band Infrared Spectroscopy | |
dc.type | Artículos de revistas | |