The structure of helokinestatin-5 and its biosynthetic precursor from Gila monster ( Heloderma suspectum) venom: Evidence for helokinestatin antagonism of bradykinin-induced relaxation of rat tail artery smooth muscle

Here we report the primary structure of a novel peptide, named helokinestatin-5 (VPPPLQMPLIPR), from the venom of the Gila monster ( Heloderma suspectum). Helokinestatin-5 differs in structure from helokinestatin-3 by deletion of a single prolyl residue in the N-terminally located polyproline region...

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Published inPeptides (New York, N.Y. : 1980) Vol. 31; no. 8; pp. 1555 - 1561
Main Authors Zhang, Yao, Wang, Lei, Zhou, Mei, Zhou, Zhihao, Chen, Xiaole, Chen, Tianbao, Kwok, HangFai, Ivanyi, Craig, Shaw, Chris
Format Journal Article
LanguageEnglish
Published New York, NY Elsevier Inc 01.08.2010
Elsevier
Subjects
Rat
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Summary:Here we report the primary structure of a novel peptide, named helokinestatin-5 (VPPPLQMPLIPR), from the venom of the Gila monster ( Heloderma suspectum). Helokinestatin-5 differs in structure from helokinestatin-3 by deletion of a single prolyl residue in the N-terminally located polyproline region. Two different biosynthetic precursors were consistently cloned from a venom-derived cDNA library. The first encoded helokinestatins 1–4 and a single copy of C-type natriuretic peptide, as previously described, whereas the second was virtually identical, lacking only a single prolyl codon as found in the mature attenuated helokinestatin-5 peptide. Helokinestatins 1–3 and 5 were synthesized by solid-phase fmoc chemistry and each synthetic replicate was found to antagonize the relaxation effect induced by bradykinin on rat tail artery smooth muscle. Helokinestatins thus represent a novel family of vasoactive peptides from the venom of helodermatid lizards.
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ISSN:0196-9781
1873-5169
DOI:10.1016/j.peptides.2010.04.030