Identification of five new bradykinin potentiating peptides (BPPs) from Bothrops jararaca crude venom by using electrospray ionization tandem mass spectrometry after a two-step liquid chromatography.
Bradykinin potentiating peptides (BPPs) from Bothrops jararaca venom were described in the middle of 1960s and were the first natural inhibitors of the angiotensin-converting enzyme displaying strong anti-hypertensive effects in human subjects. The BPPs can be recognized by their typical pyroglutamyl proline-rich oligopeptide sequences presenting invariably a proline residue at the C-terminus. In the present study, we identified 18 BPPs, most of them already described for the B. jararaca venom. We isolated and sequenced new peptides ranging from 5 to 14 amino acid residues exhibiting similar amino acid sequence features. The applied methodology consisted of a strait two-step liquid chromatography, followed by mass spectrometry analysis. Besides the amino acid sequence homology, the corresponding synthetic peptides were able to potentiate bradykinin on the isolated guinea-pig ileum.
Ianzer
Danielle
D
Center for Applied Toxinology CAT-CEPID, Instituto Butantan, Av. Vital Brasil, 1500, Sao Paulo, SP 05503-900.
Konno
Katsuhiro
K
Marques-Porto
Rafael
R
Vieira Portaro
Fernanda Calheta
FC
Stöcklin
Reto
R
Martins de Camargo
Antônio Carlos
AC
Pimenta
Daniel Carvalho
DC
D000806:Angiotensin-Converting Enzyme Inhibitors / Q000737:chemistry; D000818:Animals; D017837:Bothrops; D002850:Chromatography, Gel; D002853:Chromatography, Liquid; D009842:Oligopeptides / Q000032:analysis / Q000737:chemistry* / Q000302:isolation & purification*; D021241:Spectrometry, Mass, Electrospray Ionization; D014757:Viper Venoms / Q000032:analysis / Q000737:chemistry* / Q000302:isolation & purification
D000806:Angiotensin-Converting Enzyme Inhibitors; C571405:BPP-5a peptide, Bothrops jararaca; D009842:Oligopeptides; D014757:Viper Venoms; C006791:bradykinin potentiating factors