Cation Translocating Effects of Alamethicin and its Synthetic Fragments in Lipid Membranes: Influence of peptide chain length and charge
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Abstract
Alamethicin, a 20 residue polypeptide ionophore forms transmembrane channels and has been shown to induce excitability phenomena in artificial lipid membranes [1]. The discovery of a number of related polypeptides, containing α-aminoisobutyric acid (Aib) [2], has stimulated considerable interest in the conformational analysis of Aib peptides, with a view towards establishing the structural requirements for formation of membrane channels [3-5].