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• W2000403899 abstract "With a view toward possible new insights into viral fusion mechanisms, we have investigated the HIV-1 gp41 fusion peptide in a monomolecular film of the biomembrane lipid palmitoyloleoylphosphatidylcholine. Its surface activity at an air/water interface was measured under equilibrium conditions, using the conventional Langmuir trough technique. Through a novel thermodynamic analysis, the partial molecular area of the peptide in the lipid moiety could be determined as a function of the lateral pressure and the interfacial peptide/lipid ratio. This indicates an orientation of the peptide backbone parallel to the lipid hydrocarbon tails. The molecular area decreases significantly upon monolayer compression, suggesting a conformational transition from a somewhat compact configuration to a more extended, presumably β-strand structure when a lipid packing density is approached that is generally believed to mimic the physical state of a biological membrane. Up to a lateral pressure of ∼15 mN/m, practically all peptide inserts into the lipid monolayer. At higher compression a distinct partitioning into the aqueous subphase is observed. Under these conditions the data also reflect a strong aggregation of the lipid-associated peptide. Beyond a critical peptide/lipid ratio, the peptide's area requirement was found to become substantially enhanced, possibly because of the formation of water-filled pores." @default.
• W2000403899 created "2016-06-24" @default.
• W2000403899 creator A5025137617 @default.
• W2000403899 creator A5056059508 @default.
• W2000403899 date "1999-06-01" @default.
• W2000403899 modified "2023-10-14" @default.
• W2000403899 title "Polymorphism and Interactions of a Viral Fusion Peptide in a Compressed Lipid Monolayer" @default.
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• W2000403899 doi "https://doi.org/10.1016/s0006-3495(99)77468-0" @default.
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