Interaction of human immunodeficiency virus (HIV-1) fusion peptides with artificial lipid membranes.
The interaction of 11 overlapping synthetic peptides corresponding to N-terminal segment of HIV transmembrane glycoprotein gp41 (fusion domain) with artificial lipid membranes has been studied. For this purpose the increase of a bilayer lipid membrane (BLM) conductivity and the changes in ESR spectra of spin-labelled liposomes were registrated. Peptide fragment 523-532 gp160 (BRU strain) had the critical length with regard to channel-forming activity on BLM. The degree of such membranotropic action increased simultaneously with the growth of peptide length and the temperature in the cell. Peptides 518-532 and 517-532 lysed TEMPOcholine-containing liposomes at 37 degrees C. The significance of observed effects for explanation of the mechanism of HIV-induced membrane fusion is discussed.
Slepushkin
V A
VA
D.I. Ivanovsky Institute of Virology, Moscow, USSR.
Melikyan
G B
GB
Sidorova
M S
MS
Chumakov
V M
VM
Andreev
S M
SM
Manulyan
R A
RA
Karamov
E V
EV
D000595:Amino Acid Sequence; D004578:Electron Spin Resonance Spectroscopy; D015700:HIV Envelope Protein gp41 / Q000378:metabolism*; D015497:HIV-1 / Q000378:metabolism*; D008051:Lipid Bilayers / Q000378:metabolism*; D008564:Membrane Potentials; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis; D010713:Phosphatidylcholines / Q000378:metabolism; D010714:Phosphatidylethanolamines / Q000378:metabolism; D014760:Viral Fusion Proteins / Q000378:metabolism*
D015700:HIV Envelope Protein gp41; D008051:Lipid Bilayers; D010455:Peptides; D010713:Phosphatidylcholines; D010714:Phosphatidylethanolamines; D014760:Viral Fusion Proteins