Detail of "11017-50-8"

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Conformational requirements for the potential dependent pore formation of the peptide antibiotics alamethicin, suzukacillin and trichotoxin: Conformational requirements for the potential dependent pore formation of the peptide antibiotics alamethicin, suzukacillin and trichotoxin. Jung, G.; Katz, E.; Schmitt, H.; Voges, K. P.; Menestrina, G.; Boheim, G. (Inst. Org. Chem., Univ. Tuebingen, Tuebingen D-7400, Fed. Rep. Ger.).Several substances with their cas registry numbers 11017-50-8 and 72103-72-1 may be metioned in this study. Stud. Phys. Theor. Chem., 24(Phys. Chem. Transmembr. Ion Motions), 349-57 (English) 1983. CODEN: SPTCDZ. ISSN: 0167-6881. DOCUMENT TYPE: Journal CA Section: 34 (Amino Acids, Peptides, and Proteins) Section cross-reference(s): 22 The potential dependent ion conducting pore systems of alamethicin type polypeptide antibiotics, melittin, and synthetic peptides are based on dipole-dipole interactions of their helical parts according to the flip-flop gating model. The only structural requirement for pore formation is a rigid, lipophilic helical segment of a peptide chain as demonstrated on Me3CO2C-(L-Ala-Aib-Ala-Aib-Ala)n-OMe (Aib = NHCMe2CO,n = 1-4). .