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Peptides. 2008 Jan;29(1):65-72. Epub 2007 Nov 9.

Helokinestatin: a new bradykinin B2 receptor antagonist decapeptide from lizard venom.

Author information

1
School of Biomedical Sciences, University of Ulster, Coleraine BT52 1SA, Northern Ireland, UK. h.f.kwok@qub.ac.uk <h.f.kwok@qub.ac.uk>

Abstract

Synthetic bradykinin antagonist peptides/peptoids have been powerful tools for delineating the roles of kinins in both normal physiology and in pathological states. Here, we report the identification of a novel, naturally occurring bradykinin B2 receptor antagonist peptide, helokinestatin, isolated and structurally characterized from the venoms of helodermatid lizards-the Gila monster (Heloderma suspectum) and the Mexican beaded lizard (Heloderma horridum). The primary structure of the peptide was established by a combination of microsequencing and mass spectroscopy as Gly-Pro-Pro-Tyr-Gln-Pro-Leu-Val-Pro-Arg (Mr 1122.62). A synthetic replicate of helokinestatin was found to inhibit bradykinin-induced vasorelaxation of phenylephrine pre-constricted rat tail artery smooth muscle, mediated by the B2 receptor sub-type, in a dose-dependent manner. Natural selection, that generates functional optimization of predatory reptile venom peptides, can potentially provide new insights for drug lead design or for normal physiological or pathophysiological processes.

PMID:
18078686
DOI:
10.1016/j.peptides.2007.10.025
[Indexed for MEDLINE]

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