Membrane binding and conformational properties of peptides representing the NH2 terminus of influenza HA-2

J Biol Chem. 1987 May 15;262(14):6500-5.

Abstract

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.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Circular Dichroism
  • Hemagglutinin Glycoproteins, Influenza Virus
  • Hemagglutinins, Viral*
  • Influenza A virus / immunology*
  • Kinetics
  • Lipid Bilayers
  • Peptides / chemical synthesis*
  • Protein Conformation
  • Receptors, Virus / immunology*
  • Species Specificity
  • Spectrometry, Fluorescence

Substances

  • Hemagglutinin Glycoproteins, Influenza Virus
  • Hemagglutinins, Viral
  • Lipid Bilayers
  • Peptides
  • Receptors, Virus