ArticleThe journal of physical chemistry letters2023
Accelerating Lipid Flip-Flop at Low Concentrations: A General Mechanism for Membrane Binding Peptides.
Article in The journal of physical chemistry letters, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 11 citations in OpenAlex.
- Nanosystems for delivery of indolicidin peptide.Frontiers in medical technology · 2026Review
- AI-guided transition path sampling of lipid flip-flop and membrane nanoporation.Nature communications · 2025Article
- A Bioinspired Mastoparan Exhibits Concentration-Dependent Anti-Bacterial Activity via Membrane Disruption.ACS applied materials & interfaces · 2025Article
- Stochastic Model for the Internal Transfer Kinetics of Cargo in Carriers with Two Compartments.Membranes · 2025Article
- Structural pores not required: Antimicrobial peptides induce ion permeabilization of lipid membranes through transient water channels.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Membrane-Embedded Anti-Cancer Peptide Causes a Minimal Structural Perturbation That Is Sufficient to Enhance Phospholipid Flip-Flop and Charge Permeation Rates.Life (Basel, Switzerland) · 2025Article
- Antibiofilm Activities of Tritrpticin Analogs Against PathogenicMolecules (Basel, Switzerland) · 2025Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We report a physicochemical investigation of the lipid transport properties of model lipid membranes in the presence of the antimicrobial peptide indolicidin through comparisons of experimental SANS/SAXS scattering techniques to fully atomistic molecular dynamics simulations. In agreement with the experiment, we show that upon peripheral binding of the peptides, even at low concentrations, lipid flip-flop dynamics is greatly accelerated. Computer modeling elucidates the interplay between structural changes and lipid dynamics induced by peptides and proposes a mechanism for the mode of action of antimicrobial peptides, assessing the major role of entropy for the catalysis of the flipping events. The mechanism introduced here is universal for all peptides with preferential peripheral binding to the membrane as it does not depend on the specific amino acid sequence.
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Registered trials
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