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| Registros recuperados : 331 | |
| Registros recuperados : 331 | |
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Registro Completo
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Biblioteca(s): |
Embrapa Recursos Genéticos e Biotecnologia. |
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Data corrente: |
15/12/2015 |
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Data da última atualização: |
20/03/2023 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Circulação/Nível: |
A - 1 |
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Autoria: |
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. |
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Afiliação: |
DANIEL DIAS RUFINO ARCANJO, Universidade Federal do Piauí –UFPI; ANDREANNE GOMES VASCONCELOS, Universidade Federal do Piauí –UFPI; SIMÓN GABRIEL, Aarhus University; JOILSON RAMOS JESUS, Universidade Federal do Piauí –UFPI; LUCIANO PAULINO DA SILVA, CENARGEN; OSMINDO RODRIGUES PIRES JÚNIOR, Universidade de Brasília–UnB; CLAUDIO MIGUEL COSTA-NETO, Universidade de São Paulo–USP, Ribeirão Preto; EDUARDO BRANDT OLIVEIRA, Universidade de São Paulo–USP, Ribeirão Preto; LUDOVICO MIGLIOLO, Universidade Católica de Brasília–UCB; OCTÁVIO LUIZ FRANCO, Universidade Católica de Brasília–UCB; CAROLINA BARALDI ARAÚJO RESTINI, Universidade de Ribeirão Preto–UNAERP; MICHELE PAULO, Universidade de São Paulo–USP, Ribeirão Preto; LUSIANE MARIA BENDHACK, Universidade de São Paulo–USP, Ribeirão Preto; MARCELO PORTO BEMQUERER, CENARGEN; ALDEIDIA PEREIRA OLIVEIRA, Universidade Federal do Piauí –UFPI; ULF SIMONSEN, Aarhus University; JOSÉ ROBERTO DE SOUZA DE ALMEIDA LEITE, Universidade Federal do Piauí –UFPI. |
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Título: |
A novel vasoactive proline-rich oligopeptide from the skin secretion of the frog Brachycephalus ephippium. |
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Ano de publicação: |
2015 |
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Fonte/Imprenta: |
Plos One, v. 10, dez. 2015. (Open Access) |
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DOI: |
10.1371/journal.pone.0145071 |
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Idioma: |
Inglês |
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Conteúdo: |
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. MenosProline-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 ne... Mostrar Tudo |
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Palavras-Chave: |
Brachycephalus ephippium; Proline-rich oligopeptides. |
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Thesaurus NAL: |
secretion. |
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Categoria do assunto: |
-- |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/182309/1/journal.pone.0145071.PDF
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Marc: |
LEADER 02864naa a2200361 a 4500
001 2031700
005 2023-03-20
008 2015 bl uuuu u00u1 u #d
024 7 $a10.1371/journal.pone.0145071$2DOI
100 1 $aARCANJO, D. D. R.
245 $aA novel vasoactive proline-rich oligopeptide from the skin secretion of the frog Brachycephalus ephippium.$h[electronic resource]
260 $c2015
520 $aProline-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.
650 $asecretion
653 $aBrachycephalus ephippium
653 $aProline-rich oligopeptides
700 1 $aVASCONCELOS, A. G.
700 1 $aCOMERMA-STEFFENSEN, S. G.
700 1 $aJESUS, J. R.
700 1 $aSILVA, L. P. da
700 1 $aPIRES JÚNIOR, O. R.
700 1 $aCOSTA-NETO, C. M.
700 1 $aOLIVEIRA, E. B.
700 1 $aMIGLIOLO, L.
700 1 $aFRANCO, O. L.
700 1 $aRESTINI, C. B. A.
700 1 $aPAULO, M.
700 1 $aBENDHACK, L. M.
700 1 $aBEMQUERER, M. P.
700 1 $aOLIVEIRA, A. P.
700 1 $aSIMONSEN, U.
700 1 $aLEITE, J. R. de S. de A.
773 $tPlos One$gv. 10, dez. 2015. (Open Access)
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Embrapa Recursos Genéticos e Biotecnologia (CENARGEN) |
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