TAILIEUCHUNG - Báo cáo khoa học: A novel bradykinin potentiating peptide isolated from Bothrops jararacussu venom using catallytically inactive oligopeptidase EP24.15

Characterization of the peptide content of venoms has a number of poten-tial benefits for basic research, clinical diagnosis, development of new therapeutic agents, and production of antiserum. Here, we use a substrate-capture assay that employs a catalytically inactive mutant of thimet oligo-peptidase (EC ; ) to identify novel bioactive peptides in Bothrops jararacussu venom. | ễFEBS Journal A novel bradykinin potentiating peptide isolated from Bothrops jararacussu venom using catallytically inactive oligopeptidase Vanessa Rioli1 Benedito C. Prezoto2 Katsuhiro Konno1 Robson L. Melo1 Clécio F. Klitzke1 Emer S. Ferro3 Monica Ferreira-Lopes1 Antonio C. M. Camargo1 and Fernanda C. V. Portaro1 4 1 Laboratorio Especialde Toxinologia Aplicada-CAT CEPID Instituto Butantan Scio Paulo Brazil 2 Laboratorio Farmacologia Instituto Butantan Sao Paulo Brazil 3 Departamento de Biologia Celular e Desenvolvimento ICB USP Sao Paulo Brazil 4 Laboratorio Imunoquimica Instituto Butantan Sao Paulo Brazil Keywords angiotensin-converting enzyme blood pressure bradykinin-potentiating peptide snake venom thimet oligopeptidase Correspondence V. Rioli Laboratorio Especialde Toxinologia Aplicada - CAT CEPID Instituto Butantan Av. VitalBrasil1500 CEP05503-900 Sao Paulo Brazil Fax Tel 55 11 37261024 E-mail vrioli@ F. C. V. Portaro Laboratoi rio de Imunoquimica Instituto Butantan Av. Vital Brasil1500 CEP05503-900 Sao Paulo Brazil Fax 55 11 37267222 ext. 2106 Tel 55 11 37267222 ext. 2048 E-mail fcvportaro@ Received 4 December 2007 revised 29 January 2008 accepted 10 March 2008 doi Characterization of the peptide content of venoms has a number of potential benefits for basic research clinical diagnosis development of new therapeutic agents and production of antiserum. Here we use a substratecapture assay that employs a catalytically inactive mutant of thimet oligopeptidase EC to identify novel bioactive peptides in Bothrops jararacussu venom. Of the peptides captured with inactive and identified by mass spectrometry three were previously identified bradykinin-potentiating peptides BPP ENWPHPQIPP Xc EGGWpRPGPEIPP XIIIa and EARPpHpPIPP XIe where E is a pyroglutamyl residue . In addition we identified a novel BPP peptide containing additional AP amino acids in the C-terminus .

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