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dc.contributor.authorARCANJO, D. D. R.
dc.contributor.authorVASCONCELOS, A. G.
dc.contributor.authorCOMERMA-STEFFENSEN, S. G.
dc.contributor.authorJESUS, J. R.
dc.contributor.authorSILVA, L. P. da
dc.contributor.authorPIRES JÚNIOR, O. R.
dc.contributor.authorCOSTA-NETO, C. M.
dc.contributor.authorOLIVEIRA, E. B.
dc.contributor.authorMIGLIOLO, L.
dc.contributor.authorFRANCO, O. L.
dc.contributor.authorRESTINI, C. B. A.
dc.contributor.authorPAULO, M.
dc.contributor.authorBENDHACK, L. M.
dc.contributor.authorBEMQUERER, M. P.
dc.contributor.authorOLIVEIRA, A. P.
dc.contributor.authorSIMONSEN, U.
dc.contributor.authorLEITE, J. R. de S. de A.
dc.identifier.citationPlos One, v. 10, dez. 2015. (Open Access)
dc.descriptionProline-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.
dc.subjectProline-rich oligopeptides
dc.subjectBrachycephalus ephippium
dc.titleA novel vasoactive proline-rich oligopeptide from the skin secretion of the frog Brachycephalus ephippium.
dc.typeArtigo de periódico
dc.contributor.institutionDANIEL DIAS RUFINO ARCANJO, Universidade Federal do Piauí –UFPI
dc.contributor.institutionANDREANNE GOMES VASCONCELOS, Universidade Federal do Piauí –UFPIpt_BR
dc.contributor.institutionSIMÓN GABRIEL, Aarhus Universitypt_BR
dc.contributor.institutionJOILSON RAMOS JESUS, Universidade Federal do Piauí –UFPIpt_BR
dc.contributor.institutionLUCIANO PAULINO DA SILVA, CENARGENpt_BR
dc.contributor.institutionOSMINDO RODRIGUES PIRES JÚNIOR, Universidade de Brasília–UnBpt_BR
dc.contributor.institutionCLAUDIO MIGUEL COSTA-NETO, Universidade de São Paulo–USP, Ribeirão Pretopt_BR
dc.contributor.institutionEDUARDO BRANDT OLIVEIRA, Universidade de São Paulo–USP, Ribeirão Pretopt_BR
dc.contributor.institutionLUDOVICO MIGLIOLO, Universidade Católica de Brasília–UCBpt_BR
dc.contributor.institutionOCTÁVIO LUIZ FRANCO, Universidade Católica de Brasília–UCBpt_BR
dc.contributor.institutionCAROLINA BARALDI ARAÚJO RESTINI, Universidade de Ribeirão Preto–UNAERPpt_BR
dc.contributor.institutionMICHELE PAULO, Universidade de São Paulo–USP, Ribeirão Pretopt_BR
dc.contributor.institutionLUSIANE MARIA BENDHACK, Universidade de São Paulo–USP, Ribeirão Pretopt_BR
dc.contributor.institutionMARCELO PORTO BEMQUERER, CENARGENpt_BR
dc.contributor.institutionALDEIDIA PEREIRA OLIVEIRA, Universidade Federal do Piauí –UFPIpt_BR
dc.contributor.institutionULF SIMONSEN, Aarhus Universitypt_BR
dc.contributor.institutionJOSÉ ROBERTO DE SOUZA DE ALMEIDA LEITE, Universidade Federal do Piauí –UFPI.pt_BR
Appears in Collections:Artigo em periódico indexado (CENARGEN)

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