Interactions of the antimicrobial β‐peptide β‐17 with phospholipid vesicles differ from membrane interactions of magainins

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Abstract
We have studied the interaction of β‐17, a potent synthetic antimicrobial β‐peptide, with phospholipids. We find that unlike other antimicrobial peptides such as magainin II, β‐17 facilitates the formation of nonbilayer phases, indicating that the peptide promotes negative curvature. Studies of liposomal leakage also indicate a different mode of membrane interaction relative to magainin II, but both leakage and membrane binding show that β‐17, like magainin II, has strong affinity for membranes containing anionic lipids. This is likely to be an important factor contributing to the antimicrobial specificity of the β‐peptide.

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