Liposome destabilization induced by the HIV-1 fusion peptide effect of a single amino acid substitution.
The 23-residue synthetic peptide representing the N-terminus of HIV-1 gp41 is known to induce either leakage or fusion of lipid vesicles depending on the experimental conditions. In this paper we report that a polar amino acid substitution V-->E at position 2, known to block gp41 activity in vivo, makes the peptide unable to destabilize and/or fuse membranes. Moreover this variant, unlike the parent peptide, is never found in the membrane-associated beta conformation.
Pereira
F B
FB
Department of Biochemistry and Molecular Biology, University of the Basque Country, Bilbao, Spain.
Goñi
F M
FM
Nieva
J L
JL
D000595:Amino Acid Sequence; D015700:HIV Envelope Protein gp41 / Q000737:chemistry* / Q000494:pharmacology*; D008081:Liposomes / Q000378:metabolism*; D008561:Membrane Fusion / Q000187:drug effects; D008969:Molecular Sequence Data; D009281:Naphthalenes / Q000378:metabolism; D010446:Peptide Fragments / Q000737:chemistry / Q000494:pharmacology; D011487:Protein Conformation; D013050:Spectrometry, Fluorescence; D013329:Structure-Activity Relationship
D015700:HIV Envelope Protein gp41; D008081:Liposomes; D009281:Naphthalenes; D010446:Peptide Fragments; C046465:8-amino-1,3,6-naphthalenetrisulfonic acid