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 conforma...

Full description

Saved in:
Bibliographic Details
Published in:The Journal of biological chemistry 1987-05, Vol.262 (14), p.6500-6505
Main Authors: Lear, J D, DeGrado, W F
Format: Article
Language:English
Subjects:
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
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(18)48270-1