Any investigation on pore-forming peptides has the long-term goal to understand how the interactions between peptides and lipids influence the conformation and the orientation of both, leading eventually to membrane permeabilization. Here, we studied the lipid environment dependence of the single channel properties generated by alamethicin (Aim) F50/5 and its [L-Glu(OMe)~(7,18,19)] analog (having the Gln residues at positions 7, 18 and 19 substituted by Glu, characterized by a methyl ester group in the γ-position). Both peptides were inserted in a cell plasma membrane (recorded in whole-ceil) and in membrane patches excised from giant unilamellar vesicles (GUVs). The possibility to compare the channel activity in the precisely controlled lipid environment of GUVs, with the channel activity recorded in a natural membrane with the same ionic electrochemical gradients, will open new possibilities in the biophysical characterization of the pores.
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