Protein matrices for improved wound healing : elastase inhibition by a synthetic peptide model
Autor(a) principal: | |
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Data de Publicação: | 2010 |
Outros Autores: | , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/1822/17323 |
Resumo: | The unique properties of silk fibroin were combined with keratin to develop new wound-dressing materials. Silk fibroin/keratin (SF/K) films were prepared to reduce high levels of elastase found on chronic wounds. This improved biological function was achieved by the incorporation of a small peptide synthesized based on the reactive-site loop of the Bowman−Birk Inhibitor (BBI) protein. In vitro degradation and release were evaluated using porcine pancreatic elastase (PPE) solution as a model of wound exudate. It was found that biological degradation and release rate are highly dependent on film composition. Furthermore, the level of PPE activity can be tuned by changing the film composition, thus showing an innovative way of controlling the elastase−antielastase imbalance found on chronic wounds. |
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Protein matrices for improved wound healing : elastase inhibition by a synthetic peptide modelScience & TechnologyThe unique properties of silk fibroin were combined with keratin to develop new wound-dressing materials. Silk fibroin/keratin (SF/K) films were prepared to reduce high levels of elastase found on chronic wounds. This improved biological function was achieved by the incorporation of a small peptide synthesized based on the reactive-site loop of the Bowman−Birk Inhibitor (BBI) protein. In vitro degradation and release were evaluated using porcine pancreatic elastase (PPE) solution as a model of wound exudate. It was found that biological degradation and release rate are highly dependent on film composition. Furthermore, the level of PPE activity can be tuned by changing the film composition, thus showing an innovative way of controlling the elastase−antielastase imbalance found on chronic wounds.We would like to acknowledge FCT - Portuguese Foundation for Science and Technology for the scholarship concession; European project Lidwine, contract no. NMP2-CT-2006-026741, and Silvia Cappellozza from "Sezione Specializzata per la Bachicoltura" for the supply of silk cocoons.ACS PublicationsUniversidade do MinhoVasconcelos, AndreiaPêgo, A. P.Lamghari, M.Henriques, L.Paulo, Artur Cavaco20102010-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/17323eng1525-779710.1021/bm100537b20690591info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-07-21T12:28:03Zoai:repositorium.sdum.uminho.pt:1822/17323Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T19:22:46.571533Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse |
dc.title.none.fl_str_mv |
Protein matrices for improved wound healing : elastase inhibition by a synthetic peptide model |
title |
Protein matrices for improved wound healing : elastase inhibition by a synthetic peptide model |
spellingShingle |
Protein matrices for improved wound healing : elastase inhibition by a synthetic peptide model Vasconcelos, Andreia Science & Technology |
title_short |
Protein matrices for improved wound healing : elastase inhibition by a synthetic peptide model |
title_full |
Protein matrices for improved wound healing : elastase inhibition by a synthetic peptide model |
title_fullStr |
Protein matrices for improved wound healing : elastase inhibition by a synthetic peptide model |
title_full_unstemmed |
Protein matrices for improved wound healing : elastase inhibition by a synthetic peptide model |
title_sort |
Protein matrices for improved wound healing : elastase inhibition by a synthetic peptide model |
author |
Vasconcelos, Andreia |
author_facet |
Vasconcelos, Andreia Pêgo, A. P. Lamghari, M. Henriques, L. Paulo, Artur Cavaco |
author_role |
author |
author2 |
Pêgo, A. P. Lamghari, M. Henriques, L. Paulo, Artur Cavaco |
author2_role |
author author author author |
dc.contributor.none.fl_str_mv |
Universidade do Minho |
dc.contributor.author.fl_str_mv |
Vasconcelos, Andreia Pêgo, A. P. Lamghari, M. Henriques, L. Paulo, Artur Cavaco |
dc.subject.por.fl_str_mv |
Science & Technology |
topic |
Science & Technology |
description |
The unique properties of silk fibroin were combined with keratin to develop new wound-dressing materials. Silk fibroin/keratin (SF/K) films were prepared to reduce high levels of elastase found on chronic wounds. This improved biological function was achieved by the incorporation of a small peptide synthesized based on the reactive-site loop of the Bowman−Birk Inhibitor (BBI) protein. In vitro degradation and release were evaluated using porcine pancreatic elastase (PPE) solution as a model of wound exudate. It was found that biological degradation and release rate are highly dependent on film composition. Furthermore, the level of PPE activity can be tuned by changing the film composition, thus showing an innovative way of controlling the elastase−antielastase imbalance found on chronic wounds. |
publishDate |
2010 |
dc.date.none.fl_str_mv |
2010 2010-01-01T00:00:00Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/1822/17323 |
url |
http://hdl.handle.net/1822/17323 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
1525-7797 10.1021/bm100537b 20690591 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
ACS Publications |
publisher.none.fl_str_mv |
ACS Publications |
dc.source.none.fl_str_mv |
reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
instname_str |
Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
instacron_str |
RCAAP |
institution |
RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
collection |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
repository.name.fl_str_mv |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
repository.mail.fl_str_mv |
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1799132699755020288 |