Orientations of amphipathic helical peptides in membrane bilayers determined by solid-state NMR spectroscopy

• DOI: 10.1007/bf01877228
• Publication Date: 2005-07-04T11:07:42Z
• Authors: B. Bechinger; Y. Kim; L. E. Chirlian; J. Gesell; J. -M. Neumann; M. Montal; J. Tomich; M. Zasloff; S. J. Opella
• Keywords: Magnetic Resonance Spectroscopy; Lipid Bilayers; Molecular Sequence Data; Molecular Conformation; Membrane Proteins; Receptors, Nicotinic; Xenopus Proteins; Magainins; Ion Channels; Peptide Fragments; Membrane Lipids; Amino Acid Sequence; Peptides; Antimicrobial Cationic Peptides

Solid-state NMR spectroscopy was used to determine the orientations of two amphipathic helical peptides associated with lipid bilayers. A single spectral parameter provides sufficient orientational information for these peptides, which are known, from other methods, to be helical. The orientations of the peptides were determined using the 15N chemical shift observed for specifically labeled peptide sites. Magainin, an antibiotic peptide from frog skin, was found to lie in the plane of the bilayer. M2 delta, a helical segment of the nicotinic acetylcholine receptor, was found to span the membrane, perpendicular to the plane of the bilayer. These findings have important implications for the mechanisms of biological functions of these peptides.