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 β conformation. © 1995.
CITATION STYLE
Pereira, F. B., Goñi, F. M., & Nieva, J. L. (1995). Liposome destabilization induced by the HIV-1 fusion peptide Effect of a single amino acid substitution. FEBS Letters, 362(2), 243–246. https://doi.org/10.1016/0014-5793(95)00257-A
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