title: Structure and orientation of the antibiotic peptide magainin in membranes by solid-state nuclear magnetic resonance spectroscopy.
abstract: Magainin 2 is a 23-residue peptide that forms an amphipathic alpha-helix in membrane environments. It functions as an antibiotic and is known to disrupt the electrochemical gradients across the cell membranes of many bacteria, fungi, and some tumor cells, although it does not lyse red blood cells. One- and two-dimensional solid-state 15N NMR spectra of specifically 15N-labeled magainin 2 in oriented bilayer samples show that the secondary structure of essentially the entire peptide is alpha-helix, immobilized by its interactions with the phospholipids, and oriented parallel to the membrane surface.
authors.affiliation: Department of Chemistry, University of Pennsylvania, Philadelphia 19104.
authors.forename: B
authors.initials: B
authors.lastname: Bechinger
authors.forename: M
authors.initials: M
authors.lastname: Zasloff
authors.forename: S J
authors.initials: SJ
authors.lastname: Opella
mesh_terms: D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000737:chemistry*; D023181:Antimicrobial Cationic Peptides; D008051:Lipid Bilayers / Q000737:chemistry*; D054806:Magainins; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D029867:Xenopus Proteins
chemical_list: D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D008051:Lipid Bilayers; D054806:Magainins; D029867:Xenopus Proteins; C053301:magainin 2 peptide, Xenopus