Data/hora: 25/09/2024 19:54:52

Biblioteca(s): 	Embrapa Recursos Genéticos e Biotecnologia.	
Data corrente: 	15/12/2015	
Data da última atualização: 	20/06/2024	
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.	
Afiliação: 	DANIEL DIAS RUFINO ARCANJO, UNIVERSIDADE FEDERAL DO PIAUÍ; ANDREANNE GOMES VASCONCELOS, UNIVERSIDADE FEDERAL DO PIAUÍ; SIMÓN GABRIEL, AARHUS UNIVERSITY; JOILSON RAMOS JESUS, UNIVERSIDADE FEDERAL DO PIAUÍ; LUCIANO PAULINO DA SILVA, CENARGEN; OSMINDO RODRIGUES PIRES JÚNIOR, UNIVERSIDADE DE BRASÍLIA; CLAUDIO MIGUEL COSTA-NETO, UNIVERSIDADE DE SÃO PAULO; EDUARDO BRANDT OLIVEIRA, UNIVERSIDADE DE SÃO PAULO; LUDOVICO MIGLIOLO, UNIVERSIDADE CATÓLICA DE BRASÍLIA; OCTÁVIO LUIZ FRANCO, UNIVERSIDADE CATÓLICA DE BRASÍLIA; CAROLINA BARALDI ARAÚJO RESTINI, UNIVERSIDADE DE RIBEIRÃO PRETO; MICHELE PAULO, UNIVERSIDADE DE SÃO PAULO; LUSIANE MARIA BENDHACK, UNIVERSIDADE DE SÃO PAULO; MARCELO PORTO BEMQUERER, CENARGEN; ALDEIDIA PEREIRA OLIVEIRA, UNIVERSIDADE FEDERAL DO PIAUÍ; ULF SIMONSEN, AARHUS UNIVERSITY; JOSÉ ROBERTO DE SOUZA DE ALMEIDA LEITE, UNIVERSIDADE FEDERAL DO PIAUÍ.	
Título: 	A novel vasoactive proline-rich oligopeptide from the skin secretion of the frog Brachycephalus ephippium.	
Ano de publicação: 	2015	
Fonte/Imprenta: 	Plos One, v. 10, dez. 2015. (Open Access)	
DOI: 	10.1371/journal.pone.0145071	
Idioma: 	Inglês	
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.	
Palavras-Chave: 	Brachycephalus ephippium; Proline-rich oligopeptides.	
Thesaurus Nal: 	secretion.	
Categoria do assunto: 	--	
URL: 	http://ainfo.cnptia.embrapa.br/digital/bitstream/item/182309/1/journal.pone.0145071.PDF	
Registro original: 	Embrapa Recursos Genéticos e Biotecnologia (CENARGEN)	
Exemplares: 	CENARGEN - (36098-1) - UPC - AP - DD -  -  -  - DIS