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M9650515.TXT
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1996-03-09
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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
SOURCE: National Library of Medicine. NOTICE: This material may be
protected by Copyright Law (Title 17, U.S.Code).