Porcine skin as a source of biodegradable matrices: alkaline treatment and glutaraldehyde crosslinking
Autor(a) principal: | |
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Data de Publicação: | 2010 |
Outros Autores: | , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Polímeros (São Carlos. Online) |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-14282010000200004 |
Resumo: | In this work, the modifications promoted by alkaline hydrolysis and glutaraldehyde (GA) crosslinking on type I collagen found in porcine skin have been studied. Collagen matrices were obtained from the alkaline hydrolysis of porcine skin, with subsequent GA crosslinking in different concentrations and reaction times. The elastin content determination showed that independent of the treatment, elastin was present in the matrices. Results obtained from in vitro trypsin degradation indicated that with the increase of GA concentration and reaction time, the degradation rate decreased. From thermogravimetry and differential scanning calorimetry analysis it can be observed that the collagen in the matrices becomes more resistant to thermal degradation as a consequence of the increasing crosslink degree. Scanning electron microscopy analysis indicated that after the GA crosslinking, collagen fibers become more organized and well-defined. Therefore, the preparations of porcine skin matrices with different degradation rates, which can be used in soft tissue reconstruction, are viable. |
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Porcine skin as a source of biodegradable matrices: alkaline treatment and glutaraldehyde crosslinkingPorcine skincollagenglutaraldehyde crosslinkingIn this work, the modifications promoted by alkaline hydrolysis and glutaraldehyde (GA) crosslinking on type I collagen found in porcine skin have been studied. Collagen matrices were obtained from the alkaline hydrolysis of porcine skin, with subsequent GA crosslinking in different concentrations and reaction times. The elastin content determination showed that independent of the treatment, elastin was present in the matrices. Results obtained from in vitro trypsin degradation indicated that with the increase of GA concentration and reaction time, the degradation rate decreased. From thermogravimetry and differential scanning calorimetry analysis it can be observed that the collagen in the matrices becomes more resistant to thermal degradation as a consequence of the increasing crosslink degree. Scanning electron microscopy analysis indicated that after the GA crosslinking, collagen fibers become more organized and well-defined. Therefore, the preparations of porcine skin matrices with different degradation rates, which can be used in soft tissue reconstruction, are viable.Associação Brasileira de Polímeros2010-06-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-14282010000200004Polímeros v.20 n.2 2010reponame:Polímeros (São Carlos. Online)instname:Associação Brasileira de Polímeros (ABPol)instacron:ABPO10.1590/S0104-14282010005000013info:eu-repo/semantics/openAccessRodrigues,Fabiana T.Martins,Virginia C. A.Plepis,Ana M. G.eng2010-07-22T00:00:00Zoai:scielo:S0104-14282010000200004Revistahttp://www.scielo.br/pohttps://old.scielo.br/oai/scielo-oai.php||revista@abpol.org.br1678-51690104-1428opendoar:2010-07-22T00:00Polímeros (São Carlos. Online) - Associação Brasileira de Polímeros (ABPol)false |
dc.title.none.fl_str_mv |
Porcine skin as a source of biodegradable matrices: alkaline treatment and glutaraldehyde crosslinking |
title |
Porcine skin as a source of biodegradable matrices: alkaline treatment and glutaraldehyde crosslinking |
spellingShingle |
Porcine skin as a source of biodegradable matrices: alkaline treatment and glutaraldehyde crosslinking Rodrigues,Fabiana T. Porcine skin collagen glutaraldehyde crosslinking |
title_short |
Porcine skin as a source of biodegradable matrices: alkaline treatment and glutaraldehyde crosslinking |
title_full |
Porcine skin as a source of biodegradable matrices: alkaline treatment and glutaraldehyde crosslinking |
title_fullStr |
Porcine skin as a source of biodegradable matrices: alkaline treatment and glutaraldehyde crosslinking |
title_full_unstemmed |
Porcine skin as a source of biodegradable matrices: alkaline treatment and glutaraldehyde crosslinking |
title_sort |
Porcine skin as a source of biodegradable matrices: alkaline treatment and glutaraldehyde crosslinking |
author |
Rodrigues,Fabiana T. |
author_facet |
Rodrigues,Fabiana T. Martins,Virginia C. A. Plepis,Ana M. G. |
author_role |
author |
author2 |
Martins,Virginia C. A. Plepis,Ana M. G. |
author2_role |
author author |
dc.contributor.author.fl_str_mv |
Rodrigues,Fabiana T. Martins,Virginia C. A. Plepis,Ana M. G. |
dc.subject.por.fl_str_mv |
Porcine skin collagen glutaraldehyde crosslinking |
topic |
Porcine skin collagen glutaraldehyde crosslinking |
description |
In this work, the modifications promoted by alkaline hydrolysis and glutaraldehyde (GA) crosslinking on type I collagen found in porcine skin have been studied. Collagen matrices were obtained from the alkaline hydrolysis of porcine skin, with subsequent GA crosslinking in different concentrations and reaction times. The elastin content determination showed that independent of the treatment, elastin was present in the matrices. Results obtained from in vitro trypsin degradation indicated that with the increase of GA concentration and reaction time, the degradation rate decreased. From thermogravimetry and differential scanning calorimetry analysis it can be observed that the collagen in the matrices becomes more resistant to thermal degradation as a consequence of the increasing crosslink degree. Scanning electron microscopy analysis indicated that after the GA crosslinking, collagen fibers become more organized and well-defined. Therefore, the preparations of porcine skin matrices with different degradation rates, which can be used in soft tissue reconstruction, are viable. |
publishDate |
2010 |
dc.date.none.fl_str_mv |
2010-06-01 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-14282010000200004 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-14282010000200004 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S0104-14282010005000013 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
text/html |
dc.publisher.none.fl_str_mv |
Associação Brasileira de Polímeros |
publisher.none.fl_str_mv |
Associação Brasileira de Polímeros |
dc.source.none.fl_str_mv |
Polímeros v.20 n.2 2010 reponame:Polímeros (São Carlos. Online) instname:Associação Brasileira de Polímeros (ABPol) instacron:ABPO |
instname_str |
Associação Brasileira de Polímeros (ABPol) |
instacron_str |
ABPO |
institution |
ABPO |
reponame_str |
Polímeros (São Carlos. Online) |
collection |
Polímeros (São Carlos. Online) |
repository.name.fl_str_mv |
Polímeros (São Carlos. Online) - Associação Brasileira de Polímeros (ABPol) |
repository.mail.fl_str_mv |
||revista@abpol.org.br |
_version_ |
1754212585730736128 |