Open AccessInteractions of the antimicrobial β‐peptide β‐17 with phospholipid vesicles differ from membrane interactions of magainins
Author(s) -
Epand Raquel F.,
Umezawa Naoki,
Porter Emilie A.,
Gellman Samuel H.,
Epand Richard M.
Publication year - 2003
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1046/j.1432-1033.2003.03484.x
Subject(s) - magainin , peptide , membrane , antimicrobial , antimicrobial peptides , phospholipid , liposome , membrane curvature , biophysics , vesicle , chemistry , biochemistry , biology , organic chemistry
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.