Search results for "Alamethicin"
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The Alignment of Membrane-Active Peptides Depends on the Lipid Phase State as Viewed by solid state 19F-NMR
2009
Amphipathic membrane-active peptides (antimicrobial, hemolytic, cell-penetrating, fusogenic, etc.) achieve their functions by distinct interaction with lipid bilayers. Some typical structural modes are described in terms of models like the “barrel stave”, “toroidal pore”, “carpet” etc. These models are related to the alignment states of the peptides in the lipid bilayers (surface bound “S-state”, inserted “I-state” or tilted “T-state”), which can be readily characterized by solid state NMR. When determining such alignment, factors like peptide/lipid ratio, charge of the bilayer surface, thickness of the bilayer core, presence of cholesterol, and humidity are typically investigated. Yet, the…
Isolation and structural characterization of polypeptide antibiotics of the peptaibol class by high-performance liquid chromatography with field deso…
1984
Abstract A number of polypeptide antibiotics of the peptaibol class, i.e., trichotoxin, alamethicin, suzukacillin, hypelcin and paracelsin, have been separated into components and isolated by high-performance liquid chromatography on spherical, porous octadecylsilyl bonded phases. All peptaibols were found to reveal a strong microheterogeneity due to single or multiple amino acid exchange. Most of the closely related and partially isobaric sequence analogue could be resolved using mixed alcohol—water eluents. As demonstrated by the structure analysis of the paracelsins and the main component of trichotoxin A-50, high-performance liquid chromatography with field desorption and fast atom bomb…