Simulation of the Influenza Fusion Peptide Pre-Pore Structure

Abstract

Influenza virus dependent membrane fusion requires facilitation by a fusion peptide. Membrane deformation theory predicts that amphipathic peptide-induced lipidic pores are less stable in membranes containing lipids that generate negative spontaneous curvature, such as cholesterol. To explicitly test predictions of this theory, the membrane permeability of giant unilamellar vesicles (GUV), with and without cholesterol, were investigated experimentally using an influenza fusion peptide analog. The peptide formed stable membrane pores in POPC lipid GUVs, while pore formation was inhibited in 50:50 mol% cholesterol:POPC membranes.