ArticleJournal of the American Chemical Society2011
Helical hairpin structure of influenza hemagglutinin fusion peptide stabilized by charge-dipole interactions between the N-terminal amino group and the second helix.
Article in Journal of the American Chemical Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 38 citations in OpenAlex.
- Computational methods to study enveloped viral entry.Biochemical Society transactions · 2021Review
- Molecular mechanisms of the influenza fusion peptide: insights from experimental and simulation studies.FEBS open bio · 2021Review
- Effect of pH on the influenza fusion peptide properties unveiled by constant-pH molecular dynamics simulations combined with experiment.Scientific reports · 2020Article
- Membrane Composition Modulates Fusion by Altering Membrane Properties and Fusion Peptide Structure.The Journal of membrane biology · 2019Review
- Novel pH Selective, Highly Lytic Peptides Based on a Chimeric Influenza Hemagglutinin Peptide/Cell Penetrating Peptide Motif.Molecules (Basel, Switzerland) · 2019Article
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- Charged N-terminus of Influenza Fusion Peptide Facilitates Membrane Fusion.International journal of molecular sciences · 2018Article
- Determination of the pKScientific reports · 2017Article
- Closed and Semiclosed Interhelical Structures in Membrane vs Closed and Open Structures in Detergent for the Influenza Virus Hemagglutinin Fusion Peptide and Correlation of Hydrophobic Surface Area with Fusion Catalysis.Journal of the American Chemical Society · 2015Article
- Solution NMR studies reveal the location of the second transmembrane domain of the human sigma-1 receptor.FEBS letters · 2015Article
- The influenza hemagglutinin fusion domain is an amphipathic helical hairpin that functions by inducing membrane curvature.The Journal of biological chemistry · 2015Article
- Assembly of Influenza Hemagglutinin Fusion Peptides in a Phospholipid Bilayer by Coarse-grained Computer Simulations.Frontiers in molecular biosciences · 2015Article
- The three lives of viral fusion peptides.Chemistry and physics of lipids · 2014Review
- Structure and dynamics of a fusion peptide helical hairpin on the membrane surface: comparison of molecular simulations and NMR.The journal of physical chemistry. B · 2014Article
- The impact of influenza hemagglutinin fusion peptide length and viral subtype on its structure and dynamics.Biopolymers · 2013Review
- Lipid tail protrusion in simulations predicts fusogenic activity of influenza fusion peptide mutants and conformational models.PLoS computational biology · 2013Article
- pH-triggered, activated-state conformations of the influenza hemagglutinin fusion peptide revealed by NMR.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Unusual titration of the membrane-bound artificial hemagglutinin fusion peptide.European biophysics journal : EBJ · 2012Article
- The influenza fusion peptide adopts a flexible flat V conformation in membranes.Biophysical journal · 2012Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The fusion domain of the influenza coat protein hemagglutinin HA2, bound to dodecyl phosphocholine micelles, was recently shown to adopt a structure consisting of two antiparallel α-helices, packed in an exceptionally tight hairpin configuration. Four interhelical H(α) to C═O aliphatic H-bonds were identified as factors stabilizing this fold. Here, we report evidence for an additional stabilizing force: a strong charge-dipole interaction between the N-terminal Gly(1) amino group and the dipole moment of helix 2. pH titration of the amino-terminal (15)N resonance, using a methylene-TROSY-based 3D NMR experiment, and observation of Gly(1 13)C' show a strongly elevated pK = 8.8, considerably higher than expected for an N-terminal amino group in a lipophilic environment. Chemical shifts of three C-terminal carbonyl carbons of helix 2 titrate with the protonation state of Gly(1)-N, indicative of a close proximity between the N-terminal amino group and the axis of helix 2, providing an optimal charge-dipole stabilization of the antiparallel hairpin fold. pK values of the side-chain carboxylate groups of Glu(11) and Asp(19) are higher by about 1 and 0.5 unit, respectively, than commonly seen for solvent-exposed side chains in water-soluble proteins, indicative of dielectric constants of ε = ∼30 (Glu(11)) and ∼60 (Asp(19)), placing these groups in the headgroup region of the phospholipid micelle.
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