Tailoring elastase inhibition with synthetic peptides
Autor(a) principal: | |
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Data de Publicação: | 2011 |
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/1822/15152 |
Resumo: | Chronic wounds are the result of excessive amounts of tissue destructive proteases such as human neutrophil elastase (HNE). The high levels of this enzyme found on those types of wounds inactivate the endogenous inhibitor barrier thus, the search for new HNE inhibitors is required. This work presents two new HNE inhibitor peptides, which were synthesized based on the reactive-site loop of the Bowman–Birk inhibitor protein. The results obtained indicated that these new peptides are competitive inhibitors for HNE and, the inhibitory activity can be modulated by modifications introduced at the N- and C-terminal of the peptides. Furthermore, these peptides were also able to inhibit elastase from a human wound exudate while showing no cytotoxicity against human skin fibroblasts in vitro, greatly supporting their potential application in chronic wound treatment. |
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Tailoring elastase inhibition with synthetic peptidesHuman neutrophil elastase (HNE)Inhibition kineticBowman-Birk inhibitorPeptideWound exudateScience & TechnologyChronic wounds are the result of excessive amounts of tissue destructive proteases such as human neutrophil elastase (HNE). The high levels of this enzyme found on those types of wounds inactivate the endogenous inhibitor barrier thus, the search for new HNE inhibitors is required. This work presents two new HNE inhibitor peptides, which were synthesized based on the reactive-site loop of the Bowman–Birk inhibitor protein. The results obtained indicated that these new peptides are competitive inhibitors for HNE and, the inhibitory activity can be modulated by modifications introduced at the N- and C-terminal of the peptides. Furthermore, these peptides were also able to inhibit elastase from a human wound exudate while showing no cytotoxicity against human skin fibroblasts in vitro, greatly supporting their potential application in chronic wound treatment.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.ElsevierUniversidade do MinhoVasconcelos, AndreiaAzóia, Nuno G.Carvalho, A. C.Gomes, A. C.Guebitz, G. M.Paulo, Artur Cavaco20112011-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/15152eng0014-299910.1016/j.ejphar.2011.05.05621658384info: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:RCAAP2023-07-21T12:25:59Zoai:repositorium.sdum.uminho.pt:1822/15152Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T19:20:18.728860Repositório 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 |
Tailoring elastase inhibition with synthetic peptides |
title |
Tailoring elastase inhibition with synthetic peptides |
spellingShingle |
Tailoring elastase inhibition with synthetic peptides Vasconcelos, Andreia Human neutrophil elastase (HNE) Inhibition kinetic Bowman-Birk inhibitor Peptide Wound exudate Science & Technology |
title_short |
Tailoring elastase inhibition with synthetic peptides |
title_full |
Tailoring elastase inhibition with synthetic peptides |
title_fullStr |
Tailoring elastase inhibition with synthetic peptides |
title_full_unstemmed |
Tailoring elastase inhibition with synthetic peptides |
title_sort |
Tailoring elastase inhibition with synthetic peptides |
author |
Vasconcelos, Andreia |
author_facet |
Vasconcelos, Andreia Azóia, Nuno G. Carvalho, A. C. Gomes, A. C. Guebitz, G. M. Paulo, Artur Cavaco |
author_role |
author |
author2 |
Azóia, Nuno G. Carvalho, A. C. Gomes, A. C. Guebitz, G. M. Paulo, Artur Cavaco |
author2_role |
author author author author author |
dc.contributor.none.fl_str_mv |
Universidade do Minho |
dc.contributor.author.fl_str_mv |
Vasconcelos, Andreia Azóia, Nuno G. Carvalho, A. C. Gomes, A. C. Guebitz, G. M. Paulo, Artur Cavaco |
dc.subject.por.fl_str_mv |
Human neutrophil elastase (HNE) Inhibition kinetic Bowman-Birk inhibitor Peptide Wound exudate Science & Technology |
topic |
Human neutrophil elastase (HNE) Inhibition kinetic Bowman-Birk inhibitor Peptide Wound exudate Science & Technology |
description |
Chronic wounds are the result of excessive amounts of tissue destructive proteases such as human neutrophil elastase (HNE). The high levels of this enzyme found on those types of wounds inactivate the endogenous inhibitor barrier thus, the search for new HNE inhibitors is required. This work presents two new HNE inhibitor peptides, which were synthesized based on the reactive-site loop of the Bowman–Birk inhibitor protein. The results obtained indicated that these new peptides are competitive inhibitors for HNE and, the inhibitory activity can be modulated by modifications introduced at the N- and C-terminal of the peptides. Furthermore, these peptides were also able to inhibit elastase from a human wound exudate while showing no cytotoxicity against human skin fibroblasts in vitro, greatly supporting their potential application in chronic wound treatment. |
publishDate |
2011 |
dc.date.none.fl_str_mv |
2011 2011-01-01T00:00:00Z |
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/1822/15152 |
url |
http://hdl.handle.net/1822/15152 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
0014-2999 10.1016/j.ejphar.2011.05.056 21658384 |
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 |
Elsevier |
publisher.none.fl_str_mv |
Elsevier |
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 |
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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 |
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1799132664967462912 |