ArticleBiophysical journal2017
Charged Antimicrobial Peptides Can Translocate across Membranes without Forming Channel-like Pores.
Article in Biophysical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed.
- Dual-Channel Fluorescence Assays with Supramolecular Host-Dye Reporter Pairs for Membrane Activity Mapping of Peptides.Angewandte Chemie (International ed. in English) · 2026Article
- A unified model of transient poration induced by antimicrobial peptides.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Investigating How Lysophosphatidylcholine and Lysophosphatidylethanolamine Enhance the Membrane Permeabilization Efficacy of Host Defense Peptide Piscidin 1.The journal of physical chemistry. B · 2025Article
- Role of Peptide Associations in Enhancing the Antimicrobial Activity of Adepantins: Comparative Molecular Dynamics Simulations and Design Assessments.International journal of molecular sciences · 2024Article
- Unveiling mechanisms of antimicrobial peptide: Actions beyond the membranes disruption.Heliyon · 2024Review
- Melittin can permeabilize membranes via large transient pores.Nature communications · 2024Article
- Optimizing properties of translocation-enhancing transmembrane proteins.Biophysical journal · 2024Article
- Peptide translocation across asymmetric phospholipid membranes.Biophysical journal · 2024Article
- Molecular Dynamics Simulations of Drug-Conjugated Cell-Penetrating Peptides.Pharmaceuticals (Basel, Switzerland) · 2023Article
- Evaluation of the antileishmanial effect of polyclonal antibodies and cationic antimicrobial peptides.Pathogens and global health · 2023Article
- Heterogeneous Structural Disturbance of Cell Membrane by Peptides with Modulated Hydrophobic Properties.Pharmaceutics · 2022Article
- Tilted State Population of Antimicrobial Peptide PGLa Is Coupled to the Transmembrane Potential.Journal of chemical information and modeling · 2022Article
- Article
- Amphiphilic Gold Nanoparticles: A Biomimetic Tool to Gain Mechanistic Insights into Peptide-Lipid Interactions.Membranes · 2022Review
- Lactoferricins impair the cytosolic membrane ofeLife · 2022Article
- Integrated Design of a Membrane-Lytic Peptide-Based Intravenous Nanotherapeutic Suppresses Triple-Negative Breast Cancer.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022Article
- Real-Time Fluorescence Microscopy on LivingInternational journal of molecular sciences · 2022Article
- Not sorcery after all: Roles of multiple charged residues in membrane insertion of gasdermin-A3.Frontiers in cell and developmental biology · 2022Article
- Hydrophobic-hydrophilic Alternation: An effective Pattern to de novo Designed Antimicrobial Peptides.Current pharmaceutical design · 2022Article
- Predicting Membrane-Active Peptide Dynamics in Fluidic Lipid Membranes.Methods in molecular biology (Clifton, N.J.) · 2022Article
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No grant is acknowledged in the PubMed record.
Abstract
How can highly charged, cationic antimicrobial peptides (AMPs) translocate across hydrophobic lipid bilayers despite the prohibitive energetic penalty to do so? A common explanation has been the formation of peptide-lined channels. However, for most AMPs, no structures of membrane pores have been found despite clear evidence of membrane leakage and antimicrobial activity. The study here suggests an alternative and simple reason: for the AMP PGLa from Xenopus laevis (charge +5), such pores are not needed to explain both leakage and peptide translocation. Elevated-temperature multimicrosecond equilibrium simulations at all-atomistic level reveal that peptides spontaneously translocate across the membrane individually on a timescale of tens of microseconds, without forming pores. Both surface-bound peptides and lipids assist in the one-by-one translocation of the charged side chains. Single peptides can remain in a transmembrane orientation for many microseconds, snorkeling some charged residues to one interface and some to the opposite, but without inducing a water channel. Instead of stable pores, short-lived water bridges occur when two or three peptides connect at their termini, allowing both ion translocation and lipid flip-flop via a brushlike mechanism usually involving the C terminus of one peptide. The results here suggest that for some specific antimicrobial and other membrane active peptides, pore formation may not have to be invoked at all to explain peptide translocation and membrane permeabilization, which may explain why no channel structures for them have been determined experimentally.
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