| dc.creator | de Campos Vidal B. | |
| dc.date | 2014 | |
| dc.date | 2015-06-25T18:01:13Z | |
| dc.date | 2015-11-26T15:02:57Z | |
| dc.date | 2015-06-25T18:01:13Z | |
| dc.date | 2015-11-26T15:02:57Z | |
| dc.date.accessioned | 2018-03-28T22:13:50Z | |
| dc.date.available | 2018-03-28T22:13:50Z | |
| dc.identifier | | |
| dc.identifier | Acta Histochemica. Urban Und Fischer Verlag Jena, v. 116, n. 8, p. 1359 - 1366, 2014. | |
| dc.identifier | 651281 | |
| dc.identifier | 10.1016/j.acthis.2014.08.007 | |
| dc.identifier | http://www.scopus.com/inward/record.url?eid=2-s2.0-84918803326&partnerID=40&md5=0b77a2292a76a68352a775577956eb94 | |
| dc.identifier | http://www.repositorio.unicamp.br/handle/REPOSIP/87527 | |
| dc.identifier | http://repositorio.unicamp.br/jspui/handle/REPOSIP/87527 | |
| dc.identifier | 2-s2.0-84918803326 | |
| dc.identifier.uri | http://repositorioslatinoamericanos.uchile.cl/handle/2250/1256499 | |
| dc.description | Histological and histochemical observations support the hypothesis that collagen fibers can link to elastic fibers. However, the resulting organization of elastin and collagen type complexes and differences between these materials in terms of macromolecular orientation and frequencies of their chemical vibrational groups have not yet been solved. This study aimed to investigate the macromolecular organization of pure elastin, collagen type I and elastin-collagen complexes using polarized light DIC-microscopy. Additionally, differences and similarities between pure elastin and collagen bundles (CB) were investigated by Fourier transform-infrared (FT-IR) microspectroscopy. Although elastin exhibited a faint birefringence, the elastin-collagen complex aggregates formed in solution exhibited a deep birefringence and formation of an ordered-supramolecular complex typical of collagen chiral structure. The FT-IR study revealed elastin and CB peptide NH groups involved in different types of H-bonding. More energy is absorbed in the vibrational transitions corresponding to CH, CH2 and CH3 groups (probably associated with the hydrophobicity demonstrated by 8-anilino-1-naphtalene sulfonic acid sodium salt [ANS] fluorescence), and to νCN, δNH and ωCH2 groups of elastin compared to CB. It is assumed that the α-helix contribution to the pure elastin amide I profile is 46.8%, whereas that of the B-sheet is 20% and that unordered structures contribute to the remaining percentage. An FT-IR profile library reveals that the elastin signature within the 1360-1189cm-1 spectral range resembles that of Conex-Toray aramid fibers. | |
| dc.description | 116 | |
| dc.description | 8 | |
| dc.description | 1359 | |
| dc.description | 1366 | |
| dc.description | Aldrovani, M., Guaraldo, A.M.A., Vidal, B.C., Fluorescence, birefringence and confocal microscopy of the abdominal aorta from nonobese diabetic (NOD) mice (2007) Acta Histochem, 109, pp. 248-254 | |
| dc.description | Ayer, J.P., Elastic tissue (1964) International review of connective tissue research, 2, pp. 33-100. , Academic Press, New York and London | |
| dc.description | Braga-Vilela, A.S., Vidal, B.C., Identification of elastic fibers and lamellae in porcine pericardium and aorta by confocal, fluorescence and polarized light microscopy (2006) Acta Histochem, 108, pp. 125-132 | |
| dc.description | D'Souza, A.J., Hart, D.S., Middaugh, C.R., Gehrke, S.H., Characterization of the changes in secondary structure and architecture of elastin-mimetic triblock polypeptides during thermal gelation (2006) Macromolecules, 39, pp. 7084-7091 | |
| dc.description | Eglinton, G., Application of infrared spectroscopy to organic chemistry (1970) An introduction to spectroscopy methods for the identification of organic compounds, 1, pp. 129-141. , Pergamon Press, Oxford | |
| dc.description | Eyre, D.R., Paz, M.A., Gallop, P.M., Cross-linking in collagen and elastin (1984) Ann Rev Biochem, 53, pp. 717-748 | |
| dc.description | Fabian, H., Mäntele, W., Infrared spectroscopy of proteins (2002) Handbook of vibrational spectroscopy, pp. 3399-3425. , Wiley, Chichester, J.M. Chalmers, P.R. Griffiths (Eds.) | |
| dc.description | Fabian, H., Naumann, D., Methods to study protein folding by stopped-flow FT-IR (2004) Methods, 34, pp. 28-40 | |
| dc.description | Gibson, M.A., Kumaratilake, J.S., Cleary, E.G., Immunohistochemical and ultrastructural localization of MP78/70 (βig-h3) in extracellular matrix of developing and mature bovine tissues (1997) J Histochem Cytochem, 45, pp. 1683-1697 | |
| dc.description | Goissis, G., Suzigan, S., Parreira, D.R., Raymundo, S.R.O., Chaves, H., Hussain, K.M.K., Malhas de polipropileno recobertas por colágeno polianiÔnico ou como dupla camada com poli(cloreto de vinila) para reconstrução da parede abdominal (2001) Rev Bras Eng Biomed, 17, pp. 67-78 | |
| dc.description | Gordon, P.L., Huang, R., Lord, R.C., Yannas, I.V., The far-infrared spectrum of collagen (1974) Macromolecules, 7, pp. 954-956 | |
| dc.description | Goormaghtigh, E., Ruyssharet, J.-M., Raussens, V., Evaluation of the information content in infrared spectra for protein secondary structure determination (2006) Biophys J, 90, pp. 2946-2957 | |
| dc.description | Kielty, C.M., Sherratt, M.J., Shuttleworth, C.A., Elastic fibers (2002) J Cell Sci, 115, pp. 2817-2828 | |
| dc.description | Kumashiro, K.K., Ho, J.P., Niemczura, W.P., Keeley, F.W., Cooperativity between the hydrophobic and cross-linking domains of elastin (2006) J Biol Chem, 281, pp. 23757-23765 | |
| dc.description | Mecham, R.P., Methods in elastic tissue biology: elastin isolation and purifications (2008) Methods, 45, pp. 32-41 | |
| dc.description | Mello, M.L.S., Vidal, B.C., Anisotropic properties of toluidine blue-stained collagen (1973) Ann Histochim, 18, pp. 103-122 | |
| dc.description | Mello, M.L.S., Vidal, B.C., Analysis of the DNA Fourier transform-infrared microspectroscopic signature using an all-reflecting objective (2014) Micron, 61, pp. 49-52 | |
| dc.description | Popescu, M.-C., Vasile, C., Craciunesco, O., Structural analysis of some soluble elastins by means of FT-IR 2D IR correlation spectroscopy (2010) Biopolymers, 93, pp. 1072-1083 | |
| dc.description | Ribeiro, J.F., dos Anjos, E.H.M., Mello, M.L.S., Vidal, B.C., Skin collagen fiber molecular order: a pattern of distributional fiber orientation as assessed by optical anisotropy and image analysis (2013) PLoS One, 8, p. e54724 | |
| dc.description | Romhányi, G., Specific topo-optical reactions of connective tissue elements and their ultraestructural interpretation (1986) Connect Tissue Res, 15, pp. 13-16 | |
| dc.description | Romhányi, G., Deák, G.Y., Fischer, J., Aldhyde-bisulfite-toluidine blue (PTB) staining as a topo-optical reaction for demonstration of linear order of vicinal OH groups in biological structures (1975) Histochemistry, 43, pp. 333-348 | |
| dc.description | Silva, D.F.T., Gomes, A.S.L., Vidal, B.C., Ribeiro, M.S., Birefringence and second harmonic generation on tendon collagen following red linearly polarized laser irradiation (2013) Ann Biomed Eng, 41, pp. 752-762 | |
| dc.description | Uitto, J., Paul, J.L., Brockley, K., Pearce, R.H., Clark, J.G., Elastic fibers in human skin: quantification of elastic fibers by computerized digital image analyses and determination of elastin by radioimmunoassay of desmosine (1983) Lab Invest, 49, pp. 499-505 | |
| dc.description | Vidal, B.C., The use of 8-anilino-naphtalene sulfate (ANS) for collagen and elastin histochemistry (1978) J Histochem Cytochem, 26, pp. 196-201 | |
| dc.description | Vidal, B.C., Aorta and tendon collagen reactivity to 8-anilino-naphtalene sulfate (ANS) and dansylchloride (1980) Cell Mol Biol, 26, pp. 583-588 | |
| dc.description | Vidal, B.C., From collagen type I solution to fibers with a helical pattern: a self-assembly phenomenon (1995) CR Acad Sci Paris, Sci de la Vie, 318, pp. 831-836 | |
| dc.description | Vidal, B.C., Image analysis of tendon helical superstructure using interference and polarized light microscopy (2003) Micron, 34, pp. 423-432 | |
| dc.description | Vidal, B.C., Using the FT-IR linear dichroism method for molecular order determination of tendon collagen bundles and nylon 6 (2013) Acta Histochem, 115, pp. 686-691 | |
| dc.description | Vidal, B.C., Mello, M.L.S., Collagen type I amide I infrared spectroscopy (2011) Micron, 42, pp. 283-289 | |
| dc.description | Vidal, B.C., Ghiraldini, F.G., Mello, M.L.S., Changes in liver cell methylation status in diabetic mice affect its FT-IR characteristics (2014) PLoS One, 9, p. e102295 | |
| dc.description | Wilson, E.B., Wells, A.J., The experimental determination of the intensities of the infra-red absorption bands. 1. Theory of the methods (1946) J Chem Phys, 14, pp. 578-580 | |
| dc.description | Yugami, H., Shibayama, Y., Matsuo, S., Ishigame, M., Shin, S., Proton sites and defect-interactions in SrZrO3 single crystals studied by infrared absorption spectroscopy (1996) Solid State Ionics, 85, pp. 319-322 | |
| dc.description | Zoumi, A., Lu, X., Kassab, G.S., Tromberg, B.J., Imaging coronary artery microstructure using second-harmonic and two-photon fluorescence microscopy (2004) Biophys J, 87, pp. 2778-2786 | |
| dc.language | en | |
| dc.publisher | Urban und Fischer Verlag Jena | |
| dc.relation | Acta Histochemica | |
| dc.rights | fechado | |
| dc.source | Scopus | |
| dc.title | Fluorescence, Aggregation Properties And Ft-ir Microspectroscopy Of Elastin And Collagen Fibers | |
| dc.type | Artículos de revistas | |
