A two-dimensional NMR study of the antimicrobial peptide magainin 2.
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.
Marion
D
D
Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, MD 20892.
Zasloff
M
M
Bax
A
A
D000818:Animals; D000890:Anti-Infective Agents; D023181:Antimicrobial Cationic Peptides; D054806:Magainins; D009682:Magnetic Resonance Spectroscopy; D010455:Peptides; D011487:Protein Conformation; D012996:Solutions; D014270:Trifluoroethanol / Q000494:pharmacology; D014867:Water; D029867:Xenopus Proteins; D014982:Xenopus laevis
D000890:Anti-Infective Agents; D023181:Antimicrobial Cationic Peptides; D054806:Magainins; D010455:Peptides; D012996:Solutions; D029867:Xenopus Proteins; D014867:Water; C053301:magainin 2 peptide, Xenopus; D014270:Trifluoroethanol