ArticleBiophysical journal2008
Coarse-grained simulation studies of peptide-induced pore formation.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 81 citations in OpenAlex.
- Understanding cell-penetrating peptide mechanisms using computational electrophysiology simulations.Protein science : a publication of the Protein Society · 2026Article
- Advances in molecular dynamics approaches for investigating cell-penetrating peptides.Biophysical reviews · 2026Review
- Using multiscale molecular dynamics simulations to explore the fusion machinery underlying neurotransmitter release.Quarterly reviews of biophysics · 2025Review
- How SNARE proteins generate force to fuse membranes.Biophysical journal · 2025Article
- Coarse-grained molecular simulation of extracellular vesicle squeezing for drug loading.Physical chemistry chemical physics : PCCP · 2023Article
- Planar aggregation of the influenza viral fusion peptide alters membrane structure and hydration, promoting poration.Nature communications · 2022Article
- Finite-Size Effects in Simulations of Peptide/Lipid Assembly.The Journal of membrane biology · 2022Article
- Enhanced translocation of amphiphilic peptides across membranes by transmembrane proteins.Biophysical journal · 2021Article
- Article
- How Melittin Inserts into Cell Membrane: Conformational Changes, Inter-Peptide Cooperation, and Disturbance on the Membrane.Molecules (Basel, Switzerland) · 2019Review
- Computational studies of peptide-induced membrane pore formation.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
- Engineering monolayer poration for rapid exfoliation of microbial membranes.Chemical science · 2017Article
- Lipid somersaults: Uncovering the mechanisms of protein-mediated lipid flipping.Progress in lipid research · 2016Review
- More than the sum of its parts: coarse-grained peptide-lipid interactions from a simple cross-parametrization.The Journal of chemical physics · 2014Article
- Membrane sculpting by F-BAR domains studied by molecular dynamics simulations.PLoS computational biology · 2013Article
- Determining the Gaussian curvature modulus of lipid membranes in simulations.Biophysical journal · 2012Article
- Line-tension controlled mechanism for influenza fusion.PloS one · 2012Article
- A systematically coarse-grained solvent-free model for quantitative phospholipid bilayer simulations.The journal of physical chemistry. B · 2010Article
- Molecular interactions between magainin 2 and model membranes in situ.The journal of physical chemistry. B · 2009Article
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We investigate the interactions between lipid bilayers and amphiphilic peptides using a solvent-free coarse-grained simulation technique. In our model, each lipid is represented by one hydrophilic and three hydrophobic beads. The amphiphilic peptide is modeled as a hydrophobic-hydrophilic cylinder with hydrophilic caps. We find that with increasing peptide-lipid attraction the preferred state of the peptide changes from desorbed, to adsorbed, to inserted. A single peptide with weak attraction binds on the bilayer surface, while one with strong attraction spontaneously inserts into the bilayer. We show how several peptides, which individually bind only to the bilayer surface, cooperatively insert. Furthermore, hydrophilic strips along the peptide cylinder induce the formation of multipeptide pores, whose size and morphology depend on the peptides' overall hydrophilicity, the distribution of hydrophilic residues, and the peptide-peptide interactions. Strongly hydrophilic peptides insert less readily, but prove to be more destructive to bilayer integrity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.