A two-dimensional NMR study of the antimicrobial peptide magainin 2

FEBS Lett. 1988 Jan 18;227(1):21-6. doi: 10.1016/0014-5793(88)81405-4.

Abstract

Using two-dimensional NMR spectroscopy, a complete 1H resonance assignment has been obtained for the peptide magainin 2 recently isolated from Xenopus laevis. It is demonstrated that this peptide adopts an alpha-helical structure with amphiphilic character when dissolved in a mixture of trifluoroethanol (TFE) and H2O. The transition to the alpha-helical conformation occurs at very low concentrations of TFE.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Anti-Infective Agents
  • Antimicrobial Cationic Peptides*
  • Magainins
  • Magnetic Resonance Spectroscopy
  • Peptides*
  • Protein Conformation
  • Solutions
  • Trifluoroethanol / pharmacology
  • Water
  • Xenopus Proteins*
  • Xenopus laevis

Substances

  • Anti-Infective Agents
  • Antimicrobial Cationic Peptides
  • Magainins
  • Peptides
  • Solutions
  • Xenopus Proteins
  • Water
  • magainin 2 peptide, Xenopus
  • Trifluoroethanol