title: Fungal metabolites. XX. Effect of proline residue on the structure of ion-channel-forming peptide, trichosporin B-VIa.
abstract: The secondary structures of an ion-channel-forming icosapeptaibol, trichosporin B-VIa, and its Aib14-substituted derivative containing no Pro were investigated on the basis of CD and various NM experiments in methanol. Trichosporin B-VIa has a fully helical structure with a kink stabilized by a 1<--4 hydrogen-bond between the Leu12 CO and Val15 NH. The helical structure is composed of 3(10)-helix in the N-terminal first turn and the C-terminal moiety following Leu12, and alpha-helix in the middle region. In contrast, the Aib14 derivative predominantly has a straight alpha-helical structure except for a 3(10)-helix region in the N-terminal first turn.
authors.affiliation: Faculty of Pharmaceutical Sciences, Kyoto University, Japan.
authors.forename: Y
authors.initials: Y
authors.lastname: Nagaoka
authors.forename: A
authors.initials: A
authors.lastname: Iida
authors.forename: E
authors.initials: E
authors.lastname: Tachikawa
authors.forename: T
authors.initials: T
authors.lastname: Fujita
mesh_terms: D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000737:chemistry*; D023181:Antimicrobial Cationic Peptides; D002942:Circular Dichroism; D003903:Deuterium; D005656:Fungal Proteins / Q000737:chemistry* / Q000502:physiology; D007473:Ion Channels / Q000737:chemistry* / Q000502:physiology; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D010455:Peptides; D011392:Proline / Q000737:chemistry* / Q000502:physiology; D017433:Protein Structure, Secondary; D014242:Trichoderma / Q000378:metabolism*
chemical_list: D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D005656:Fungal Proteins; D007473:Ion Channels; D010455:Peptides; C089061:trichosporin B-VIa; D011392:Proline; D003903:Deuterium