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

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