Liposome destabilization induced by the HIV‐1 fusion peptide Effect of a single amino acid substitution

[摘要]

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.

[学科分类] 生物化学/生物物理

[关键词] Membrane fusion;Fusion peptide;Peptide conformation;HIV-1;ANTS;8-aminonaphtalene-1;3;6-trisulfonic acid;DMSO;dimethylsulfoxide;DPX;p-xylenebis(pyridinium)bromide;FTIR;Fourier transform infrared spectroscopy;HEPES;N-(2-hydroxyethhyl)-piperazine-N′-2-ethanesulfonic acid;HIV;human immunodeficiency virus HIVwt;synthetic N-terminal sequence (23 aa) of HIV-1 gp41;HIVE2 synthetic N-terminal sequence (23 aa) of HIV-1 gp41 bearing the V→E substitution at position 2;LUV;large unilamellar vesicles;N-NBD-PE;N-(7-nitrobenz-2-oxa-1;3-diazol-4-yl)phosphatidylethanolamine;PC;phosphatidylcholine;PE;phosphatidylethanolamine;POPG;1-palmitoyl-2-oleoylphosphatidylglycerol;N-Rh-PE;N-(lissamine rhodamine B sulfonyl)phosphatidylethanolamine