Please use this identifier to cite or link to this item: http://www.alice.cnptia.embrapa.br/alice/handle/doc/1031700
Research center of Embrapa/Collection: Embrapa Recursos Genéticos e Biotecnologia - Artigo em periódico indexado (ALICE)
Date Issued: 2015
Type of Material: Artigo em periódico indexado (ALICE)
Authors: 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.
Additional Information: DANIEL DIAS RUFINO ARCANJO, Universidade Federal do Piauí –UFPI
OSMINDO RODRIGUES PIRES JÚNIOR, Universidade de Brasília–UnB
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
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.
Title: A novel vasoactive proline-rich oligopeptide from the skin secretion of the frog Brachycephalus ephippium.
Publisher: Plos One, v. 10, dez. 2015. (Open Access)
Language: en
Keywords: Proline-rich oligopeptides
Brachycephalus ephippium
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.
NAL Thesaurus: secretion
Data Created: 2015-12-15
Appears in Collections:Artigo em periódico indexado (CENARGEN)

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