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| Registros recuperados : 161 | |
| 1. |  | SARMENTO, R. B. C.; PEREIRA, M.; LAUMAN, R.; FRANCO, O. L.; VALADARES-INGLIS, M. C. Análise da patogenicidade de isolados dos fungos Beauveria bassiana e Metarhizium anisopliae var. anisopliae o carruncho de feijão de corda (Callosobruchus maculatus). In: ENCONTRO DO TALENTO ESTUDANTIL DA EMBRAPA RECURSOS GENÉTICOS E BIOTECNOLOGIA, 9., 2004, Brasília, DF. Anais: resumos dos trabalhos. Brasília, DF: Embrapa Recursos Genéticos e Biotecnologia, 2004. p. 110.| Biblioteca(s): Embrapa Recursos Genéticos e Biotecnologia. |
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| 2. | | MURAD, A. M.; MOLINARI, H. B. C.; TAKAHASHI, F.; FRANCO, O. L.; QUIRINO, B. F. Análises proteômicas e fisiológicas em Saccharum spp. submetidas a estresse salino. In: SIMPÓSIO BRASILEIRO DE RECURSOS GENÉTICOS, 2., 2008, Brasília, DF. Anais... Brasília, DF: Embrapa Recursos Genéticos e Biotecnologia, 2008. p. 105.| Biblioteca(s): Embrapa Agroenergia. |
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| 3. | | MURAD, A. M.; NORONHA, E. F.; MEHTA, A.; LAUMANN, R. A.; FRANCO, O. L. Beauveria bassiana proteomics: understanding fungi-host mechanisms for development of novel strategies on Callosobruchus maculatus biocontrol. In: REUNIÃO ANUAL DA SOCIEDADE BRASILEIRA DE BIOQUÍMICA E BIOLOGIA MOLECULAR, 35., 2006, Águas de Lindóia, SP. Programas e resumos... São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular, 2006. Não paginado.| Biblioteca(s): Embrapa Recursos Genéticos e Biotecnologia. |
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| 5. | | SARMENTO, R. B. C.; MARTINS, I.; LAUMANN, R.; FRANCO, O. L.; VALADARES-INGLIS, M. C. Mortalidade de caruncho de feijão de corda (Callosobruchus maculatus), causada pelos fungos entomopatogênicos Beauveria bassiana e Metarhizium anisopliae var. anisopliae. In: ENCONTRO DO TALENTO ESTUDANTIL DA EMBRAPA RECURSOS GENÉTICOS E BIOTECNOLOGIA, 8., 2003, Brasília, DF. Anais: resumos dos trabalhos. Brasília, DF: Embrapa Recursos Genéticos e Biotecnologia, 2003. p. 117.| Biblioteca(s): Embrapa Recursos Genéticos e Biotecnologia. |
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| 7. | | FRANCO, O. L.; RIGDEN, D. J.; MELO, F. R.; GROSSI-DE-SÁ, M. F. Plant alpha-amylase inhibitors and their interaction with insect alfa-amylases: structure, function and potential for crop protection. European Journal of Biochemistry, New York, NY, v. 269, n. 2, p. 397-412, 2002.| Biblioteca(s): Embrapa Recursos Genéticos e Biotecnologia. |
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| 8. | | LIMA, T. B.; GROSSI DE SÁ, M. F.; FRANCO, O. L.; LEONARDECZ, E. Phytochemistry characterization of the effect of Cagaita (Eugenia dysenterica) in laxative and antidiarreic compound. In: ANNUAL MEETING OF THE SBBq, 36.; IUBMB CONFERENCE, 10., 2007, Salvador, BA. Infectious diseases: biochemistry of parasites, vectors and hosts. [S.l.]: SBBq, 2007. Não paginado.| Biblioteca(s): Embrapa Recursos Genéticos e Biotecnologia. |
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| 10. | | SATO, J. H.; TEIXEIRA, J. B.; EIRA, M. T. S.; FRANCO, O. L.; MEHTA, A. Comparative proteomic analysis of Coffea arabica somatic embryos in the different stages of embryogenesis. In: INTERNATIONAL CONFERENCE ON COFFEE SCIENCE, 22., 2008, Campinas, Brazil. Programme abstracts. Montpellier, France: Association for Science and Information on Coffee, 2008. PB650.| Biblioteca(s): Embrapa Recursos Genéticos e Biotecnologia. |
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| 15. | | KOSOSKI, R. M.; REIS JÚNIOR, F. B.; FRANCO, O. L.; ROCHA, T. L.; MEHTA, A. Proteoma de Xanthomonas campestris pv. campestris na interação com genótipos resistente e suscetível de Brassica oleracea. Fitopatologia Brasileira, Brasília, DF, v. 32, S310, ago. 2007. Suplemento. Trabalho apresentado no 49. Congresso Brasileiro de Fitopatologia, 2007, Maringá, PR.| Biblioteca(s): Embrapa Cerrados; Embrapa Recursos Genéticos e Biotecnologia. |
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| 16. | | SATO, J. H.; TEIXEIRA, J. B.; EIRA, M. T. S.; FRANCO, O. L.; MEHTA, A. Proteômica comparativa em embriões somáticos de Coffea arabica nas diferentes fases da embriogênese. In: ENCONTRO DO TALENTO ESTUDANTIL DA EMBRAPA RECURSOS GENÉTICOS E BIOTECNOLOGIA, 13., 2008, Brasília, DF. Anais: resumos dos trabalhos. Brasília, DF: Embrapa Recursos Genéticos e Biotecnologia, 2008. Resumo 050. p. 90.| Biblioteca(s): Embrapa Recursos Genéticos e Biotecnologia. |
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| Registros recuperados : 161 | |
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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: |
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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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