title: 15N and 31P solid-state NMR investigations on the orientation of zervamicin II and alamethicin in phosphatidylcholine membranes.
abstract: The topologies of zervamicin II and alamethicin, labeled with (15)N uniformly, selectively, or specifically, have been investigated by oriented proton-decoupled (15)N solid-state NMR spectroscopy. Whereas at lipid-to-peptide (L/P) ratios of 50 (wt/wt) zervamicin II exhibits transmembrane alignments in 1,2-dicapryl (di-C10:0-PC) and 1,2-dilauroyl (di-C12:0-PC) phosphatidylcholine bilayers, it adopts orientations predominantly parallel to the membrane surface when the lengths of the fatty acyl chains are extended. The orientational order of zervamicin II increases with higher phospholipid concentrations, and considerable line narrowing is obtained in di-C10:0-PC/zervamicin II membranes at L/P ratios of 100 (wt/wt). In contrast to zervamicin, alamethicin is transmembrane throughout most, if not all, of its length when reconstituted into 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine bilayers. The (31)P solid-state NMR spectra of all phospholipid/peptaibol samples investigated show a high degree of headgroup order, indicating that the peptides do not distort the bilayer structure. The observed differences in peptide orientation between zervamicin and alamethicin are discussed with reference to differences in their lengths, helical conformations, distribution of (hydroxy)proline residues, and hydrophobic moments. Possible implications for peptaibol voltage-gating are also described.
authors.affiliation: Max-Planck-Institut für Biochemie, Am Klopferspitz 18A, 82152 Martinsried, Germany. bechinge@biochem.mpg.de
authors.forename: B
authors.initials: B
authors.lastname: Bechinger
authors.forename: D A
authors.initials: DA
authors.lastname: Skladnev
authors.forename: A
authors.initials: A
authors.lastname: Ogrel
authors.forename: X
authors.initials: X
authors.lastname: Li
authors.forename: E V
authors.initials: EV
authors.lastname: Rogozhkina
authors.forename: T V
authors.initials: TV
authors.lastname: Ovchinnikova
authors.forename: J D
authors.initials: JD
authors.lastname: O'Neil
authors.forename: J
authors.initials: J
authors.lastname: Raap
mesh_terms: D000408:Alamethicin / Q000737:chemistry*; D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000737:chemistry*; D006999:Hypocreales / Q000737:chemistry; D008051:Lipid Bilayers / Q000737:chemistry*; D008969:Molecular Sequence Data; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D054848:Peptaibols; D010455:Peptides; D010713:Phosphatidylcholines / Q000737:chemistry*; D010759:Phosphorus Isotopes; D011522:Protons; D014867:Water
chemical_list: D000900:Anti-Bacterial Agents; D008051:Lipid Bilayers; D009587:Nitrogen Isotopes; D054848:Peptaibols; D010455:Peptides; D010713:Phosphatidylcholines; D010759:Phosphorus Isotopes; D011522:Protons; D014867:Water; D000408:Alamethicin; C077077:zervamicin IIB; C051145:zervamicin IIA; C028694:1-palmitoyl-2-oleoylphosphatidylcholine