Novel natriuretic peptides from the venom of the inland taipan (Oxyuranus microlepidotus): Isolation, chemical and biological characterisation

Bryan G. Fry, Janith C. Wickramaratana, Scott Lemme, Anne Beuve, David Garbers, Wayne C. Hodgson, Paul Alewood

Research output: Contribution to journalArticlepeer-review

55 Scopus citations

Abstract

Three natriuretic-like peptides (TNP-a, TNP-b, and TNP-c) were isolated from the venom of Oxyuranus microlepidotus (inland taipan) and were also present in the venoms of Oxyuranus scutellatus canni (New Guinea taipan) and Oxyuranus scutellatus scutellatus (coastal taipan). They were isolated by HPLC, characterised by mass spectrometry and Edman analysis, and consist of 35-39 amino acid residues. These molecules differ from ANP/BNP through replacement of invariant residues within the 17-membered ring structure and by inclusion of proline residues in the C-terminal tail. TNP-c was equipotent to ANP in specific GC-A assays or aortic ring assays whereas TNP-a and TNP-b were either inactive (GC-A over-expressing cells and endothelium-denuded aortic rings) or weakly active (endothelium-intact aortic rings). TNP-a and TNP-b were also unable to competitively inhibit the binding of TNP-c in endothelium-denuded aortae (GC-A) or endothelium-intact aortae (NPR-C). Thus, these naturally occurring isoforms provide a new platform for further investigation of structure-function relationships of natriuretic peptides.

Original languageEnglish (US)
Pages (from-to)1011-1015
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume327
Issue number4
DOIs
StatePublished - Feb 25 2005
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Keywords

  • Guanylyl cyclase
  • Mass spectrometry
  • Natriuretic peptide
  • Oxyuranus microlepidotus
  • Venom

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