title: Testing topological models for the membrane penetration of the fusion peptide of influenza virus hemagglutinin.
abstract: Low pH-induced binding of the bromelain-solubilized form of influenza virus hemagglutinin (BHA) to membranes occurs through the fusion peptide. From asymmetric hydrophobic photolabeling of membranes, evidence was obtained that this peptide penetrates only one leaflet of the bilayer. The asymmetrical labeling was achieved by employing a photoreactive analogue of a fatty acid whose transbilayer distribution can be manipulated by a membrane proton gradient.
authors.affiliation: Department of Biochemistry, Swiss Federal Institute of Technology ETH, Zürich, Switzerland.
authors.forename: J
authors.initials: J
authors.lastname: Brunner
mesh_terms: D001963:Bromelains / Q000494:pharmacology; D005227:Fatty Acids; D006389:Hemagglutinins, Viral; D006863:Hydrogen-Ion Concentration; D008051:Lipid Bilayers; D008563:Membrane Lipids; D008954:Models, Biological; D009975:Orthomyxoviridae; D010777:Photochemistry; D014760:Viral Fusion Proteins
chemical_list: D005227:Fatty Acids; D006389:Hemagglutinins, Viral; D008051:Lipid Bilayers; D008563:Membrane Lipids; D014760:Viral Fusion Proteins; D001963:Bromelains