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• W2024690637 startingPage "e1002950" @default.
• W2024690637 abstract "Fusion peptides from influenza hemagglutinin act on membranes to promote membrane fusion, but the mechanism by which they do so remains unknown. Recent theoretical work has suggested that contact of protruding lipid tails may be an important feature of the transition state for membrane fusion. If this is so, then influenza fusion peptides would be expected to promote tail protrusion in proportion to the ability of the corresponding full-length hemagglutinin to drive lipid mixing in fusion assays. We have performed molecular dynamics simulations of influenza fusion peptides in lipid bilayers, comparing the X-31 influenza strain against a series of N-terminal mutants. As hypothesized, the probability of lipid tail protrusion correlates well with the lipid mixing rate induced by each mutant. This supports the conclusion that tail protrusion is important to the transition state for fusion. Furthermore, it suggests that tail protrusion can be used to examine how fusion peptides might interact with membranes to promote fusion. Previous models for native influenza fusion peptide structure in membranes include a kinked helix, a straight helix, and a helical hairpin. Our simulations visit each of these conformations. Thus, the free energy differences between each are likely low enough that specifics of the membrane environment and peptide construct may be sufficient to modulate the equilibrium between them. However, the kinked helix promotes lipid tail protrusion in our simulations much more strongly than the other two structures. We therefore predict that the kinked helix is the most fusogenic of these three conformations." @default.
• W2024690637 created "2016-06-24" @default.
• W2024690637 creator A5036519166 @default.
• W2024690637 creator A5081016259 @default.
• W2024690637 date "2013-03-07" @default.
• W2024690637 modified "2023-10-03" @default.
• W2024690637 title "Lipid Tail Protrusion in Simulations Predicts Fusogenic Activity of Influenza Fusion Peptide Mutants and Conformational Models" @default.
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• W2024690637 doi "https://doi.org/10.1371/journal.pcbi.1002950" @default.
• W2024690637 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3591293" @default.
• W2024690637 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23505359" @default.
• W2024690637 hasPublicationYear "2013" @default.
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