Use este identificador para citar ou linkar para este item: http://www.alice.cnptia.embrapa.br/alice/handle/doc/1031700
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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.date.accessioned2018-09-01T00:44:46Z-
dc.date.available2018-09-01T00:44:46Z-
dc.date.created2015-12-15
dc.date.issued2015
dc.identifier.citationPlos One, v. 10, dez. 2015. (Open Access)
dc.identifier.urihttp://www.alice.cnptia.embrapa.br/alice/handle/doc/1031700-
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.language.isoengeng
dc.rightsopenAccesseng
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.date.updated2018-09-01T00:44:46Zpt_BR
dc.subject.nalthesaurussecretion
riaa.ainfo.id1031700
riaa.ainfo.lastupdate2018-08-31
dc.identifier.doi10.1371/journal.pone.0145071
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
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