Liposome destabilization induced by the HIV-1 fusion peptide effect of a single amino acid substitution

F B Pereira; F M Goñi; J L Nieva

doi:10.1016/0014-5793(95)00257-a

Liposome destabilization induced by the HIV-1 fusion peptide effect of a single amino acid substitution

FEBS Lett. 1995 Apr 3;362(2):243-6. doi: 10.1016/0014-5793(95)00257-a.

Authors

F B Pereira¹, F M Goñi, J L Nieva

Affiliation

¹ Department of Biochemistry and Molecular Biology, University of the Basque Country, Bilbao, Spain.

PMID: 7720880
DOI: 10.1016/0014-5793(95)00257-a

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
HIV Envelope Protein gp41 / chemistry*
HIV Envelope Protein gp41 / pharmacology*
Liposomes / metabolism*
Membrane Fusion / drug effects
Molecular Sequence Data
Naphthalenes / metabolism
Peptide Fragments / chemistry
Peptide Fragments / pharmacology
Protein Conformation
Spectrometry, Fluorescence
Structure-Activity Relationship

Substances

HIV Envelope Protein gp41
Liposomes
Naphthalenes
Peptide Fragments
8-amino-1,3,6-naphthalenetrisulfonic acid