Solution structure and membrane interaction mode of an antimicrobial peptide gaegurin 4

Biochem Biophys Res Commun. 2007 Jan 19;352(3):592-7. doi: 10.1016/j.bbrc.2006.11.064. Epub 2006 Nov 27.


We have applied NMR spectroscopy to determine the high-resolution structure of gaegurin 4, a 37-residue antimicrobial peptide from Rana rugosa, under varying hydrophobic conditions. Even in 100% H2O, gaegurin 4 contains a nascent turn near its C-terminal Rana box. Under a more hydrophobic condition it forms two amphipathic helices, one long encompassing residues 2-23 and the other consisting of residues 25-34, similar to what has been observed in cecropin A. Functional implication of the helix-breaking kink at Gly24 in gaegurin 4 was investigated by preparing several analogs. Based upon the current and previous results, we propose a novel seaanemone-like ion pore-forming model for gaegurin 4.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Antimicrobial Cationic Peptides / chemistry
  • Cell Membrane / chemistry*
  • Computer Simulation
  • Magnetic Resonance Spectroscopy
  • Models, Chemical*
  • Models, Molecular*
  • Molecular Sequence Data
  • Protein Conformation
  • Protein Precursors / chemistry*
  • Protein Precursors / ultrastructure*
  • Solutions


  • Antimicrobial Cationic Peptides
  • Protein Precursors
  • Solutions
  • gaegurin 4