Ion-channels of cyclic template-assembled alamethicins that emulate the pore structure predicted by the barrel-stave model

Single channel measurements of cyclic template-assembled synthetic peptides (TASP) Aln-cyclo2n[AL = Ac-UPUAUAQUVUGLUPVUUG-, U =α-aminoisobutyric acid; cyclo2n=cyclo(-Lys-Abz-)n, Abz =m-aminobenzoic acid] in lipid bilayer membranes reveal that the lowest and the next lowest conductance states of the alamethicin ion-channel are made up of three and four parallel helices, respectively, as predicted by the barrel-stave model.