FEBS Letters, vol. 362, issue 2 (1995) pp. 243-246
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 ?? conformation. ?? 1995.
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