6533b7d9fe1ef96bd126b9a4
RESEARCH PRODUCT
Hexapeptides that interfere with HIV-1 fusion peptide activity in liposomes block GP41-mediated membrane fusion
Nerea HuarteJosé L. NievaIsmael MingarroMaría J. GómaraEnrique Pérez-payáMaier Lorizatesubject
CellBiophysicsMembrane fusionCHO CellsGp41BiochemistryFusion peptideMembranes (Biologia)Structural BiologyCricetinaeGeneticsmedicineNuclear fusionAnimalsMolecular BiologyFusion inhibitorFusionLiposomeChemistryLipid bilayer fusionViral fusionCell Biologygp41HIV Envelope Protein gp41Cell biologyMembranemedicine.anatomical_structureBiochemistryLiposomesHIV-1PèptidsPeptidesFusion peptidedescription
AbstractUpon receptor-mediated activation, the gp41 hydrophobic, conserved fusion peptide inserts into the target membrane and promotes the kind of perturbations required for the progression of the HIV-cell fusion reaction. Using a synthetic combinatorial library we have identified all d-amino acid hexapeptide sequences that inhibited the fusion peptide capacity of perturbing model membranes. Two hexapeptides that effectively inhibited the fusion peptide in these systems were subsequently shown to inhibit cell–cell fusion promoted by gp41 expressed at cell surfaces. These observations might be of importance for understanding the mechanisms underlying fusion peptide activity and suggest new strategies for screening compounds that target these viral sequences.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2006-01-01 |