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Alamethicin, a member of the peptaibol family of antibiotics, is a typical channel-forming peptide with a helical structure. The self-assembly of the peptide in the membranes yields voltage-dependent channels. In this study, three alamethicin analogs possessing a charged residue (His, Lys, or Glu) on their N-termini were designed with the expectation of stabilizing the transmembrane structure. A slight...
We report that long-chain poly-l-glutamine forms cation-selective channels when incorporated into artificial planar lipid bilayer membranes. The channel was permeable to alkali cations and H+ ions and virtually impermeable to anions; the selectivity sequence based on the single-channel conductance was H+ ≫ Cs+>K+>Na+. The cation channel was characterized by long-lived open states (often lasting...
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