Membrane binding and conformational properties of peptides representing the NH2 terminus of influenza HA-2.
Synthetic peptides representing amino acid residues 1-16 and 1-20, a proposed fusogenic region of the HA-2 subunit of influenza virus hemagglutinin, bind to phosphatidylcholine vesicles with submicromolar dissociation constants. The 1-20, but not the 1-16, peptide appears to adopt a helical conformation when bound to vesicles and cooperatively promotes vesicle fusion.
D000595:Amino Acid Sequence; D002942:Circular Dichroism; D019267:Hemagglutinin Glycoproteins, Influenza Virus; D006389:Hemagglutinins, Viral; D009980:Influenza A virus / Q000276:immunology*; D007700:Kinetics; D008051:Lipid Bilayers; D010455:Peptides / Q000138:chemical synthesis*; D011487:Protein Conformation; D011991:Receptors, Virus / Q000276:immunology*; D013045:Species Specificity; D013050:Spectrometry, Fluorescence
D019267:Hemagglutinin Glycoproteins, Influenza Virus; D006389:Hemagglutinins, Viral; D008051:Lipid Bilayers; D010455:Peptides; D011991:Receptors, Virus