A novel vasoactive proline-rich oligopeptide from the skin secretion of the frog Brachycephalus ephippium.

Detalhes bibliográficos
Autor(a) principal: ARCANJO, D. D. R.
Data de Publicação: 2015
Outros Autores: VASCONCELOS, A. G., COMERMA-STEFFENSEN, S. G., JESUS, J. R., SILVA, L. P. da, PIRES JÚNIOR, O. R., COSTA-NETO, C. M., OLIVEIRA, E. B., MIGLIOLO, L., FRANCO, O. L., RESTINI, C. B. A., PAULO, M., BENDHACK, L. M., BEMQUERER, M. P., OLIVEIRA, A. P., SIMONSEN, U., LEITE, J. R. de S. de A.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice)
Texto Completo: http://www.alice.cnptia.embrapa.br/alice/handle/doc/1031700
Resumo: Proline-rich oligopeptides (PROs) are a large family which comprises the bradykinin-potentiating peptides (BPPs). They inhibit the activity of the angiotensin I-converting enzyme (ACE) and have a typical pyroglutamyl (Pyr)/proline-rich structure at the N- and C-terminus, respectively. Furthermore, PROs decrease blood pressure in animals. In the present study, the isolation and biological characterization of a novel vasoactive BPP isolated from the skin secretion of the frog Brachycephalus ephippium is described. This new PRO, termed BPP-Brachy, has the primary structure WPPPKVSP and the amidated form termed BPPBrachyNH2 inhibits efficiently ACE in rat serum. In silico molecular modeling and docking studies suggest that BPP-BrachyNH2 is capable of forming a hydrogen bond network as well as multiple van der Waals interactions with the rat ACE, which blocks the access of the substrate to the C-domain active site. Moreover, in rat thoracic aorta BPP-BrachyNH2 induces potent endothelium-dependent vasodilatation with similar magnitude as captopril. In DAF-FM DA-loaded aortic cross sections examined by confocal microscopy, BPP-BrachyNH2 was found to increase the release of nitric oxide (NO). Moreover, BPP-BrachyNH2 was devoid of toxicity in endothelial and smooth muscle cell cultures. In conclusion, the peptide BPP-BrachyNH2 has a novel sequence being the first BPP isolated from the skin secretion of the Brachycephalidae family. This opens for exploring amphibians as a source of new biomolecules. The BPP-BrachyNH2 is devoid of cytotoxicity and elicits endothelium-dependent vasodilatation mediated by NO. These findings open for the possibility of potential application of these peptides in the treatment of endothelial dysfunction and cardiovascular diseases.
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spelling A novel vasoactive proline-rich oligopeptide from the skin secretion of the frog Brachycephalus ephippium.Proline-rich oligopeptidesBrachycephalus ephippiumsecretionProline-rich oligopeptides (PROs) are a large family which comprises the bradykinin-potentiating peptides (BPPs). They inhibit the activity of the angiotensin I-converting enzyme (ACE) and have a typical pyroglutamyl (Pyr)/proline-rich structure at the N- and C-terminus, respectively. Furthermore, PROs decrease blood pressure in animals. In the present study, the isolation and biological characterization of a novel vasoactive BPP isolated from the skin secretion of the frog Brachycephalus ephippium is described. This new PRO, termed BPP-Brachy, has the primary structure WPPPKVSP and the amidated form termed BPPBrachyNH2 inhibits efficiently ACE in rat serum. In silico molecular modeling and docking studies suggest that BPP-BrachyNH2 is capable of forming a hydrogen bond network as well as multiple van der Waals interactions with the rat ACE, which blocks the access of the substrate to the C-domain active site. Moreover, in rat thoracic aorta BPP-BrachyNH2 induces potent endothelium-dependent vasodilatation with similar magnitude as captopril. In DAF-FM DA-loaded aortic cross sections examined by confocal microscopy, BPP-BrachyNH2 was found to increase the release of nitric oxide (NO). Moreover, BPP-BrachyNH2 was devoid of toxicity in endothelial and smooth muscle cell cultures. In conclusion, the peptide BPP-BrachyNH2 has a novel sequence being the first BPP isolated from the skin secretion of the Brachycephalidae family. This opens for exploring amphibians as a source of new biomolecules. The BPP-BrachyNH2 is devoid of cytotoxicity and elicits endothelium-dependent vasodilatation mediated by NO. These findings open for the possibility of potential application of these peptides in the treatment of endothelial dysfunction and cardiovascular diseases.DANIEL DIAS RUFINO ARCANJO, UNIVERSIDADE FEDERAL DO PIAUÍANDREANNE GOMES VASCONCELOS, UNIVERSIDADE FEDERAL DO PIAUÍSIMÓN GABRIEL, AARHUS UNIVERSITYJOILSON RAMOS JESUS, UNIVERSIDADE FEDERAL DO PIAUÍLUCIANO PAULINO DA SILVA, CENARGENOSMINDO RODRIGUES PIRES JÚNIOR, UNIVERSIDADE DE BRASÍLIACLAUDIO MIGUEL COSTA-NETO, UNIVERSIDADE DE SÃO PAULOEDUARDO BRANDT OLIVEIRA, UNIVERSIDADE DE SÃO PAULOLUDOVICO MIGLIOLO, UNIVERSIDADE CATÓLICA DE BRASÍLIAOCTÁVIO LUIZ FRANCO, UNIVERSIDADE CATÓLICA DE BRASÍLIACAROLINA BARALDI ARAÚJO RESTINI, UNIVERSIDADE DE RIBEIRÃO PRETOMICHELE PAULO, UNIVERSIDADE DE SÃO PAULOLUSIANE MARIA BENDHACK, UNIVERSIDADE DE SÃO PAULOMARCELO PORTO BEMQUERER, CENARGENALDEIDIA PEREIRA OLIVEIRA, UNIVERSIDADE FEDERAL DO PIAUÍULF SIMONSEN, AARHUS UNIVERSITYJOSÉ ROBERTO DE SOUZA DE ALMEIDA LEITE, UNIVERSIDADE FEDERAL DO PIAUÍ.ARCANJO, D. D. R.VASCONCELOS, A. G.COMERMA-STEFFENSEN, S. G.JESUS, J. R.SILVA, L. P. daPIRES JÚNIOR, O. R.COSTA-NETO, C. M.OLIVEIRA, E. B.MIGLIOLO, L.FRANCO, O. L.RESTINI, C. B. A.PAULO, M.BENDHACK, L. M.BEMQUERER, M. P.OLIVEIRA, A. P.SIMONSEN, U.LEITE, J. R. de S. de A.2018-09-01T00:44:46Z2018-09-01T00:44:46Z2015-12-1520152018-09-01T00:44:46Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlePlos One, v. 10, dez. 2015. (Open Access)http://www.alice.cnptia.embrapa.br/alice/handle/doc/103170010.1371/journal.pone.0145071enginfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice)instname:Empresa Brasileira de Pesquisa Agropecuária (Embrapa)instacron:EMBRAPA2018-09-01T00:44:53Zoai:www.alice.cnptia.embrapa.br:doc/1031700Repositório InstitucionalPUBhttps://www.alice.cnptia.embrapa.br/oai/requestcg-riaa@embrapa.bropendoar:21542018-09-01T00:44:53Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice) - Empresa Brasileira de Pesquisa Agropecuária (Embrapa)false
dc.title.none.fl_str_mv A novel vasoactive proline-rich oligopeptide from the skin secretion of the frog Brachycephalus ephippium.
title A novel vasoactive proline-rich oligopeptide from the skin secretion of the frog Brachycephalus ephippium.
spellingShingle A novel vasoactive proline-rich oligopeptide from the skin secretion of the frog Brachycephalus ephippium.
ARCANJO, D. D. R.
Proline-rich oligopeptides
Brachycephalus ephippium
secretion
title_short A novel vasoactive proline-rich oligopeptide from the skin secretion of the frog Brachycephalus ephippium.
title_full A novel vasoactive proline-rich oligopeptide from the skin secretion of the frog Brachycephalus ephippium.
title_fullStr A novel vasoactive proline-rich oligopeptide from the skin secretion of the frog Brachycephalus ephippium.
title_full_unstemmed A novel vasoactive proline-rich oligopeptide from the skin secretion of the frog Brachycephalus ephippium.
title_sort A novel vasoactive proline-rich oligopeptide from the skin secretion of the frog Brachycephalus ephippium.
author ARCANJO, D. D. R.
author_facet ARCANJO, D. D. R.
VASCONCELOS, A. G.
COMERMA-STEFFENSEN, S. G.
JESUS, J. R.
SILVA, L. P. da
PIRES JÚNIOR, O. R.
COSTA-NETO, C. M.
OLIVEIRA, E. B.
MIGLIOLO, L.
FRANCO, O. L.
RESTINI, C. B. A.
PAULO, M.
BENDHACK, L. M.
BEMQUERER, M. P.
OLIVEIRA, A. P.
SIMONSEN, U.
LEITE, J. R. de S. de A.
author_role author
author2 VASCONCELOS, A. G.
COMERMA-STEFFENSEN, S. G.
JESUS, J. R.
SILVA, L. P. da
PIRES JÚNIOR, O. R.
COSTA-NETO, C. M.
OLIVEIRA, E. B.
MIGLIOLO, L.
FRANCO, O. L.
RESTINI, C. B. A.
PAULO, M.
BENDHACK, L. M.
BEMQUERER, M. P.
OLIVEIRA, A. P.
SIMONSEN, U.
LEITE, J. R. de S. de A.
author2_role author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv DANIEL DIAS RUFINO ARCANJO, UNIVERSIDADE FEDERAL DO PIAUÍ
ANDREANNE GOMES VASCONCELOS, UNIVERSIDADE FEDERAL DO PIAUÍ
SIMÓN GABRIEL, AARHUS UNIVERSITY
JOILSON RAMOS JESUS, UNIVERSIDADE FEDERAL DO PIAUÍ
LUCIANO PAULINO DA SILVA, CENARGEN
OSMINDO RODRIGUES PIRES JÚNIOR, UNIVERSIDADE DE BRASÍLIA
CLAUDIO MIGUEL COSTA-NETO, UNIVERSIDADE DE SÃO PAULO
EDUARDO BRANDT OLIVEIRA, UNIVERSIDADE DE SÃO PAULO
LUDOVICO MIGLIOLO, UNIVERSIDADE CATÓLICA DE BRASÍLIA
OCTÁVIO LUIZ FRANCO, UNIVERSIDADE CATÓLICA DE BRASÍLIA
CAROLINA BARALDI ARAÚJO RESTINI, UNIVERSIDADE DE RIBEIRÃO PRETO
MICHELE PAULO, UNIVERSIDADE DE SÃO PAULO
LUSIANE MARIA BENDHACK, UNIVERSIDADE DE SÃO PAULO
MARCELO PORTO BEMQUERER, CENARGEN
ALDEIDIA PEREIRA OLIVEIRA, UNIVERSIDADE FEDERAL DO PIAUÍ
ULF SIMONSEN, AARHUS UNIVERSITY
JOSÉ ROBERTO DE SOUZA DE ALMEIDA LEITE, UNIVERSIDADE FEDERAL DO PIAUÍ.
dc.contributor.author.fl_str_mv ARCANJO, D. D. R.
VASCONCELOS, A. G.
COMERMA-STEFFENSEN, S. G.
JESUS, J. R.
SILVA, L. P. da
PIRES JÚNIOR, O. R.
COSTA-NETO, C. M.
OLIVEIRA, E. B.
MIGLIOLO, L.
FRANCO, O. L.
RESTINI, C. B. A.
PAULO, M.
BENDHACK, L. M.
BEMQUERER, M. P.
OLIVEIRA, A. P.
SIMONSEN, U.
LEITE, J. R. de S. de A.
dc.subject.por.fl_str_mv Proline-rich oligopeptides
Brachycephalus ephippium
secretion
topic Proline-rich oligopeptides
Brachycephalus ephippium
secretion
description Proline-rich oligopeptides (PROs) are a large family which comprises the bradykinin-potentiating peptides (BPPs). They inhibit the activity of the angiotensin I-converting enzyme (ACE) and have a typical pyroglutamyl (Pyr)/proline-rich structure at the N- and C-terminus, respectively. Furthermore, PROs decrease blood pressure in animals. In the present study, the isolation and biological characterization of a novel vasoactive BPP isolated from the skin secretion of the frog Brachycephalus ephippium is described. This new PRO, termed BPP-Brachy, has the primary structure WPPPKVSP and the amidated form termed BPPBrachyNH2 inhibits efficiently ACE in rat serum. In silico molecular modeling and docking studies suggest that BPP-BrachyNH2 is capable of forming a hydrogen bond network as well as multiple van der Waals interactions with the rat ACE, which blocks the access of the substrate to the C-domain active site. Moreover, in rat thoracic aorta BPP-BrachyNH2 induces potent endothelium-dependent vasodilatation with similar magnitude as captopril. In DAF-FM DA-loaded aortic cross sections examined by confocal microscopy, BPP-BrachyNH2 was found to increase the release of nitric oxide (NO). Moreover, BPP-BrachyNH2 was devoid of toxicity in endothelial and smooth muscle cell cultures. In conclusion, the peptide BPP-BrachyNH2 has a novel sequence being the first BPP isolated from the skin secretion of the Brachycephalidae family. This opens for exploring amphibians as a source of new biomolecules. The BPP-BrachyNH2 is devoid of cytotoxicity and elicits endothelium-dependent vasodilatation mediated by NO. These findings open for the possibility of potential application of these peptides in the treatment of endothelial dysfunction and cardiovascular diseases.
publishDate 2015
dc.date.none.fl_str_mv 2015-12-15
2015
2018-09-01T00:44:46Z
2018-09-01T00:44:46Z
2018-09-01T00:44:46Z
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 Plos One, v. 10, dez. 2015. (Open Access)
http://www.alice.cnptia.embrapa.br/alice/handle/doc/1031700
10.1371/journal.pone.0145071
identifier_str_mv Plos One, v. 10, dez. 2015. (Open Access)
10.1371/journal.pone.0145071
url http://www.alice.cnptia.embrapa.br/alice/handle/doc/1031700
dc.language.iso.fl_str_mv eng
language eng
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
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dc.source.none.fl_str_mv reponame:Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice)
instname:Empresa Brasileira de Pesquisa Agropecuária (Embrapa)
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instname_str Empresa Brasileira de Pesquisa Agropecuária (Embrapa)
instacron_str EMBRAPA
institution EMBRAPA
reponame_str Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice)
collection Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice)
repository.name.fl_str_mv Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice) - Empresa Brasileira de Pesquisa Agropecuária (Embrapa)
repository.mail.fl_str_mv cg-riaa@embrapa.br
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