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 pyroglutamy...

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Veröffentlicht in:Peptides (New York, N.Y. : 1980) N.Y. : 1980), 2004-07, Vol.25 (7), p.1085-1092
Hauptverfasser: Ianzer, Danielle, Konno, Katsuhiro, Marques-Porto, Rafael, Vieira Portaro, Fernanda Calheta, Stöcklin, Reto, Martins de Camargo, Antônio Carlos, Pimenta, Daniel Carvalho
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Sprache:eng
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Zusammenfassung: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.
ISSN:0196-9781
1873-5169
DOI:10.1016/j.peptides.2004.04.006