title: Solution structure and membrane interaction mode of an antimicrobial peptide gaegurin 4.
abstract: We have applied NMR spectroscopy to determine the high-resolution structure of gaegurin 4, a 37-residue antimicrobial peptide from Rana rugosa, under varying hydrophobic conditions. Even in 100% H2O, gaegurin 4 contains a nascent turn near its C-terminal Rana box. Under a more hydrophobic condition it forms two amphipathic helices, one long encompassing residues 2-23 and the other consisting of residues 25-34, similar to what has been observed in cecropin A. Functional implication of the helix-breaking kink at Gly24 in gaegurin 4 was investigated by preparing several analogs. Based upon the current and previous results, we propose a novel seaanemone-like ion pore-forming model for gaegurin 4.
authors.affiliation: Molecular Cancer Research Center, Division of Molecular Therapeutics, KRIBB, Daejeon 305-806, Republic of Korea.
authors.forename: Seung-Wook
authors.initials: SW
authors.lastname: Chi
authors.forename: Jae-Sung
authors.initials: JS
authors.lastname: Kim
authors.forename: Do-Hyoung
authors.initials: DH
authors.lastname: Kim
authors.forename: Si-Hyung
authors.initials: SH
authors.lastname: Lee
authors.forename: Yong-Ha
authors.initials: YH
authors.lastname: Park
authors.forename: Kyou-Hoon
authors.initials: KH
authors.lastname: Han
mesh_terms: D000595:Amino Acid Sequence; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry; D002462:Cell Membrane / Q000737:chemistry*; D003198:Computer Simulation; D009682:Magnetic Resonance Spectroscopy; D008956:Models, Chemical; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011498:Protein Precursors / Q000737:chemistry* / Q000648:ultrastructure*; D012996:Solutions
chemical_list: D023181:Antimicrobial Cationic Peptides; D011498:Protein Precursors; D012996:Solutions; C096396:gaegurin 4