Yao Zhang

Publications (1)2.43 Total impact

• Article: 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.

  Yao Zhang, Lei Wang, Mei Zhou, Zhihao Zhou, Xiaole Chen, Tianbao Chen, HangFai Kwok, Craig Ivanyi, Chris Shaw
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  ABSTRACT: 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.
  Peptides 05/2010; 31(8):1555-61. · 2.43 Impact Factor