Identification of novel bradykinin-potentiating peptides (BPPs) in the venom gland of a rattlesnake allowed the evaluation of the structure-function relationship of BPPs

Identification of novel bradykinin-potentiating peptides (BPPs) in the venom gland of a rattlesnake allowed the evaluation of the structure-function relationship of BPPs

Author Gomes, Claudiana L. Google Scholar
Konno, Katsuhiro Google Scholar
Conceição, Isaltino Marcelo da Autor UNIFESP Google Scholar
Ianzer, Danielle Google Scholar
Yamanouye, Norma Google Scholar
Prezoto, Benedito C. Google Scholar
Assakura, Marina T. Google Scholar
Radis-Baptista, Gandhi Google Scholar
Yamane, Tetsuo Google Scholar
Santos, Robson A. Google Scholar
Camargo, Antonio C. M. de Google Scholar
Hayashi, Mirian A. F. Google Scholar
Institution Universidade Federal de São Paulo (UNIFESP)
Inst Butantan
Universidade Federal de Pernambuco (UFPE)
Universidade de São Paulo (USP)
Universidade Federal de Minas Gerais (UFMG)
Abstract Aiming to extend the knowledge about the diversity of bradykinin-potentiating peptides (BPPs) and their precursor proteins, a venom gland cDNA library from the South American rattlesnake (Crotalus dursissus terrificus, Cdt) was screened. Two novel homologous cDNAs encoding the BPPs precursor protein were cloned. Their sequence contain only one single longer BPP sequence with the typical IPP-tripeptide, and two short potential BPP-like molecules, revealing a unique structural organization. Several peptide sequences structurally similar to the BPPs identified in the precursor protein from Cdt and also from others snakes, were chemically synthesized and were bioassayed both in Uitro and in Viuo, by means of isolated smooth muscle preparations and by measurements of blood pressure in anaesthetized rats, respectively. We demonstrate here that a pyroglutamyl residue at the Nterminus with a high content of proline residues, even with the presence of a IPP moiety characteristic of typical BPPs, are not enough to determine a bradykinin-potentiating activity to these peptides. Taken together, our results indicate that the characterization of the BPPs precursor proteins and identification of characteristic glutamine residues followed by proline-rich peptide sequences are not enough to predict if these peptides, even with a pyroglutamyl residue at the N-terminus, will present the typical pharmacological activities described for the BPPs. (C) 2007 Elsevier Inc. All rights reserved.
Keywords snake venom
bradykinin-potentiating peptides
ACE inhibitors
bioactive peptides
blood pressure
toxin
Language English
Date 2007-11-01
Published in Biochemical Pharmacology. Oxford: Pergamon-Elsevier B.V., v. 74, n. 9, p. 1350-1360, 2007.
ISSN 0006-2952 (Sherpa/Romeo, impact factor)
Publisher Elsevier B.V.
Extent 1350-1360
Origin http://dx.doi.org/10.1016/j.bcp.2007.07.014
Access rights Closed access
Type Article
Web of Science ID WOS:000250663900004
URI http://repositorio.unifesp.br/handle/11600/30122

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