ArticleScientific reports2020
Effect of pH on the influenza fusion peptide properties unveiled by constant-pH molecular dynamics simulations combined with experiment.
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 23 citations in OpenAlex.
- Membrane Fusion-Inspired Nanomaterials: Emerging Strategies for Infectious Disease and Cancer Diagnostics.Advanced healthcare materials · 2026Review
- Review
- Revealing pH-dependent antimicrobial peptide, GL13K, characteristics: A constant pH molecular dynamics study.bioRxiv : the preprint server for biology · 2025Article
- Unravelling the role of key amino acid residues of the parainfluenza fusion peptide in membrane fusion.RSC chemical biology · 2025Article
- Integrating Cryo-Electron Microscopy and Molecular Dynamics Simulations to Investigate Membrane Binding of Influenza Virus Fusion Peptides.Journal of the American Chemical Society · 2025Article
- CFrontiers in microbiology · 2025Article
- Molecular Dynamics Investigation of the Influenza Hemagglutinin Conformational Changes in Acidic pH.The journal of physical chemistry. B · 2024Article
- PKAD-2: New entries and expansion of functionalities of the database of experimentally measured pKa's of proteins.Journal of computational biophysics and chemistry · 2023Article
- Two modes of fusogenic action for influenza virus fusion peptide.PLoS computational biology · 2023Article
- Constant pH molecular dynamics simulations: Current status and recent applications.Current opinion in structural biology · 2022Review
- FixBox: A General Algorithm to Fix Molecular Systems in Periodic Boxes.Journal of chemical information and modeling · 2022Article
- Parainfluenza Fusion Peptide Promotes Membrane Fusion by Assembling into Oligomeric Porelike Structures.ACS chemical biology · 2022Article
- Membrane-Bound Configuration and Lipid Perturbing Effects of Hemagglutinin Subunit 2 N-Terminus Investigated by Computer Simulations.Frontiers in molecular biosciences · 2022Article
- 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
- Transient Excursions to Membrane Core as Determinants of Influenza Virus Fusion Peptide Activity.International journal of molecular sciences · 2021Article
- Modulatory Effects of Acidic pH and Membrane Potential on the Adsorption of pH-Sensitive Peptides to Anionic Lipid Membrane.Membranes · 2021Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The influenza virus fusion process, whereby the virus fuses its envelope with the host endosome membrane to release the genetic material, takes place in the acidic late endosome environment. Acidification triggers a large conformational change in the fusion protein, hemagglutinin (HA), which enables the insertion of the N-terminal region of the HA2 subunit, known as the fusion peptide, into the membrane of the host endosome. However, the mechanism by which pH modulates the molecular properties of the fusion peptide remains unclear. To answer this question, we performed the first constant-pH molecular dynamics simulations of the influenza fusion peptide in a membrane, extending for 40 µs of aggregated time. The simulations were combined with spectroscopic data, which showed that the peptide is twofold more active in promoting lipid mixing of model membranes at pH 5 than at pH 7.4. The realistic treatment of protonation introduced by the constant-pH molecular dynamics simulations revealed that low pH stabilizes a vertical membrane-spanning conformation and leads to more frequent contacts between the fusion peptide and the lipid headgroups, which may explain the increase in activity. The study also revealed that the N-terminal region is determinant for the peptide's effect on the membrane.
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