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dc.contributor.CRUESPUNIVERSIDADE DE ESTADUAL DE CAMPINASpt_BR
dc.typeArtigo de periódicopt_BR
dc.titleFluorescence, Aggregation Properties And Ft-ir Microspectroscopy Of Elastin And Collagen Fibers.pt_BR
dc.contributor.authorVidal, Benedicto de Campospt_BR
unicamp.authorBenedicto de Campos Vidal, Department of Structural and Functional Biology, Institute of Biology, University of Campinas (Unicamp), Rua Monteiro Lobato 255, CEP 013083-862 Campinas, SP, Brazil. Electronic address: camposvi@unicamp.br.pt_BR
dc.subjectBirefringencept_BR
dc.subjectCollagen Bundlespt_BR
dc.subjectCollagen Type Ipt_BR
dc.subjectElastinpt_BR
dc.subjectFt-irpt_BR
dc.subjectHydrophobicitypt_BR
dc.description.abstractHistological 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.en
dc.relation.ispartofActa Histochemicapt_BR
dc.relation.ispartofabbreviationActa Histochem.pt_BR
dc.date.issued2014-Octpt_BR
dc.identifier.citationActa Histochemica. v. 116, n. 8, p. 1359-66, 2014-Oct.pt_BR
dc.language.isoengpt_BR
dc.description.volume116pt_BR
dc.description.firstpage1359-66pt_BR
dc.rightsfechadopt_BR
dc.rights.holderCopyright © 2014 Elsevier GmbH. All rights reserved.pt_BR
dc.sourcePubMedpt_BR
dc.identifier.issn1618-0372pt_BR
dc.identifier.doi10.1016/j.acthis.2014.08.007pt_BR
dc.identifier.urlhttp://www.ncbi.nlm.nih.gov/pubmed/25213809pt_BR
dc.date.available2015-11-27T13:43:21Z-
dc.date.accessioned2015-11-27T13:43:21Z-
dc.description.provenanceMade available in DSpace on 2015-11-27T13:43:21Z (GMT). No. of bitstreams: 1 pmed_25213809.pdf: 2516019 bytes, checksum: b8f782e6e55ca146e76ca69f66648637 (MD5) Previous issue date: 2014en
dc.identifier.urihttp://repositorio.unicamp.br/jspui/handle/REPOSIP/201720-
dc.identifier.idPubmed25213809pt_BR
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