Solution structure of a defensin-like peptide from platypus venom Academic Article uri icon


  • Three defensin-like peptides (DLPs) were isolated from platypus venom and sequenced. One of these peptides, DLP-1, was synthesized chemically and its three-dimensional structure was determined using NMR spectroscopy. The main structural elements of this 42-residue peptide were an anti-parallel β-sheet comprising residues 15-18 and 37-40 and a small 310 helix spanning residues 10-12. The overall three-dimensional fold is similar to that of β-defensin-12, and similar to the sodium-channel neurotoxin ShI (Stichodactyla helianthusneurotoxin I). However, the side chains known to be functionally important in β-defensin-12 and ShI are not conserved in DLP-1, suggesting that it has a different biological function. Consistent with this contention, we showed that DLP-1 possesses no anti-microbial properties and has no observable activity on rat dorsal-root-ganglion sodium-channel currents.


  • TORRES, Allan M
  • WANG, Xiuhong
  • FLETCHER, Jamie I
  • ALEWOOD, Dianne
  • ALEWOOD, Paul F
  • SMITH, Ross
  • SIMPSON, Richard J
  • NICHOLSON, Graham M
  • SUTHERLAND, Struan K
  • GALLAGHER, Cliff H
  • KING, Glenn F
  • KUCHEL, Philip W

publication date

  • August 1, 1999