Document 0515
 DOCN  M9650515
 TI    [Fusion of negatively-charged liposomes under the effect of peptides
       from the N-terminal fragment of the HIV-1 transmembrane protein]
 DT    9605
 AU    Terletskaia IaT; Trikash IO; Serdiuk ES; Andreev SM
 SO    Biokhimiia. 1995 Oct;60(10):1711-9. Unique Identifier : AIDSLINE
       MED/96098219
 AB    The effect of a series of synthetic peptides mimicking the N-terminus of
       HIV transmembrane glycoprotein (gp41) on fusion of negatively charged
       liposomes consisting of phosphatidylcholine, phosphatidylethanolamine
       and cardiolipin at a 2:3:5 molar ratio, respectively, has been studied.
       Peptides P514 and P385 (residue 517-538), lysine and arginine at the
       C-terminus, respectively, with the amino acid sequence completely
       corresponding to the N-terminus of gp41 displayed the highest fusogenic
       activity. The extent of fusion was significantly increased at mild
       acidic pH (6.0). Acidification particularly influenced the fusogenic
       activity of P514. Modification of the N- and C-termini of fusion-active
       peptides by proteins and synthetic polymers blocked the fusion activity.
       The fusogenic properties of peptides depended on the chain length: P411
       consisting of nine hydrophobic amino acid residues had no fusogenic
       activity, while P415, an 11-member peptide, effectively fused liposomes.
       The fluorescent probe ANS was used to monitor the hydrophobicity of
       these peptides. The hydrophobicity of P514 increased appreciably with a
       change in pH from 6.0 to 7.5. Peptides P514 and P385 induced the leakage
       of the aqueous contents from liposomes at neutral pH and caused a small,
       but detectable leakage at acidic pH. Structural and molecular factors
       influencing the peptide-induced liposome fusion are discussed.
 DE    Amino Acid Sequence  English Abstract  Hydrogen-Ion Concentration  HIV
       Envelope Protein gp41/*CHEMISTRY  HIV-1/*CHEMISTRY  *Liposomes
       Molecular Sequence Data  Peptide Fragments/*CHEMISTRY  JOURNAL ARTICLE

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