ArticleBiophysical journal2013
Fusion peptides promote formation of bilayer cubic phases in lipid dispersions. An x-ray diffraction study.
Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 43 citations in OpenAlex.
- The Interplay of Lipids and Peptides in Membrane Merger.Advances in experimental medicine and biology · 2026Review
- The local variation of the Gaussian modulus enables different pathways for fluid lipid vesicle fusion.Scientific reports · 2024Article
- Initiation and evolution of pores formed by influenza fusion peptides probed by lysolipid inclusion.Biophysical journal · 2023Article
- Planar aggregation of the influenza viral fusion peptide alters membrane structure and hydration, promoting poration.Nature communications · 2022Article
- Remodeling of the Plasma Membrane by Surface-Bound Protein Monomers and Oligomers: The Critical Role of Intrinsically Disordered Regions.The Journal of membrane biology · 2022Review
- The interaction of viral fusion peptides with lipid membranes.Biophysical journal · 2022Article
- Mechanism of Membrane Fusion: Interplay of Lipid and Peptide.The Journal of membrane biology · 2022Review
- [SARS-COV2, variants, membranes and basic physics].Bulletin de l'Academie nationale de medecine · 2022Article
- Computational methods to study enveloped viral entry.Biochemical Society transactions · 2021Review
- Imidazolium-Linked Azido-Functionalized Guerbet Glycosides: Multifunctional Surfactants for Biofunctionalization of Vesicles.ACS omega · 2019Article
- The 2018 biomembrane curvature and remodeling roadmap.Journal of physics D: Applied physics · 2018Article
- Influenza M2 Transmembrane Domain Senses Membrane Heterogeneity and Enhances Membrane Curvature.Langmuir : the ACS journal of surfaces and colloids · 2016Article
- Viral fusion protein transmembrane domain adopts β-strand structure to facilitate membrane topological changes for virus-cell fusion.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- The influenza hemagglutinin fusion domain is an amphipathic helical hairpin that functions by inducing membrane curvature.The Journal of biological chemistry · 2015Article
- The three lives of viral fusion peptides.Chemistry and physics of lipids · 2014Review
- Conformation and lipid interaction of the fusion peptide of the paramyxovirus PIV5 in anionic and negative-curvature membranes from solid-state NMR.Journal of the American Chemical Society · 2014Article
- Wild-type and mutant hemagglutinin fusion peptides alter bilayer structure as well as kinetics and activation thermodynamics of stalk and pore formation differently: mechanistic implications.Biophysical journal · 2013Article
- Importance of the hexagonal lipid phase in biological membrane organization.Frontiers in plant science · 2013Article
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
Small angle x-ray diffraction revealed a strong influence of the N-terminal influenza hemagglutinin fusion peptide on the formation of nonlamellar lipid phases. Comparative measurements were made on a series of three peptides, a 20-residue wild-type X-31 influenza virus fusion peptide, GLFGAIAGFIENGWEGMIDG, and its two point-mutant, fusion-incompetent peptides G1E and G13L, in mixtures with hydrated phospholipids, either dipalmitoleoylphosphatidylethanolamine (DPoPE), or monomethylated dioleoyl phosphatidylethanolamine (DOPE-Me), at lipid/peptide molar ratios of 200:1 and 50:1. All three peptides suppressed the HII phase and shifted the L(α)-H(II) transition to higher temperatures, simultaneously promoting formation of inverted bicontinuous cubic phases, Q(II), which becomes inserted between the L(α) and H(II) phases on the temperature scale. Peptide-induced Q(II) had strongly reduced lattice constants in comparison to the Q(II) phases that form in pure lipids. Q(II) formation was favored at the expense of both L(α) and H(II) phases. The wild-type fusion peptide, WT-20, was distinguished from G1E and G13L by the markedly greater magnitude of its effect. WT-20 disordered the L(α) phase and completely abolished the HII phase in DOPE-Me/WT-20 50:1 dispersions, converted the Q(II) phase type from Im3m to Pn3m and reduced the unit cell size from ∼38 nm for the Im3m phase of DOPE-Me dispersions to ∼15 nm for the Pn3m phase in DOPE-Me/WT-20 peptide mixtures. The strong reduction of the cubic phase lattice parameter suggests that the fusion-promoting WT-20 peptide may function by favoring bilayer states of more negative gaussian curvature and promoting fusion along pathways involving Pn3m phase-like fusion pore intermediates rather than pathways involving H(II) phase-like intermediates.
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