ArticleJournal of the American Chemical Society2014
Highly efficient macromolecule-sized poration of lipid bilayers by a synthetically evolved peptide.
Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed.
- Mechanism-Driven Screening of Membrane-Targeting and Pore-Forming Antimicrobial Peptides.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Dual-Channel Fluorescence Assays with Supramolecular Host-Dye Reporter Pairs for Membrane Activity Mapping of Peptides.Angewandte Chemie (International ed. in English) · 2026Article
- Engineering a single-chain immunoglobulin scaffold loaded with a latent-releasable cytotoxic pore-forming peptide.Communications biology · 2025Article
- Antimicrobial peptide class that forms discrete β-barrel stable pores anchored by transmembrane helices.Nature communications · 2025Article
- Conformational dynamics and molecular interactions of natural products: unveiling functional structures in biological membranes.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2025Review
- The difference between MelP5 and melittin membrane poration.Scientific reports · 2025Article
- Permeability Benchmarking: Guidelines for ComparingJournal of chemical information and modeling · 2025Review
- pH-Responsive Peptide Nanoparticles Deliver Macromolecules to Cells via Endosomal Membrane Nanoporation.ACS nano · 2024Article
- Structural Determinants of Peptide Nanopore Formation.ACS nano · 2024Article
- Plasma membrane damage limits cytoplasmic delivery by conventional cell penetrating peptides.PloS one · 2024Article
- The Functionality of Membrane-Inserting Proteins and Peptides: Curvature Sensing, Generation, and Pore Formation.The Journal of membrane biology · 2023Review
- The reduced-charge melittin analogue MelP5 improves the transfection of non-viral DNA nanoparticles.Journal of peptide science : an official publication of the European Peptide Society · 2022Article
- Atomic force microscopy for quantitative understanding of peptide-induced lipid bilayer remodeling.Methods (San Diego, Calif.) · 2022Article
- Predicting Membrane-Active Peptide Dynamics in Fluidic Lipid Membranes.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Synthetic Molecular Evolution of Cell Penetrating Peptides.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Applications and evolution of melittin, the quintessential membrane active peptide.Biochemical pharmacology · 2021Review
- Membrane-selective nanoscale pores in liposomes by a synthetically evolved peptide: implications for triggered release.Nanoscale · 2021Article
- pH-triggered pore-forming peptides with strong composition-dependent membrane selectivity.Biophysical journal · 2021Article
- Tuning of a Membrane-Perforating Antimicrobial Peptide to Selectively Target Membranes of Different Lipid Composition.The Journal of membrane biology · 2021Article
- Antimicrobial Peptides and Proteins: From Nature's Reservoir to the Laboratory and Beyond.Frontiers in chemistry · 2021Review
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Authors and funding
6 authors.
Funding
Abstract
Peptides that self-assemble, at low concentration, into bilayer-spanning pores which allow the passage of macromolecules would be beneficial in multiple areas of biotechnology. However, there are few, if any, natural or designed peptides that have this property. Here we show that the 26-residue peptide "MelP5", a synthetically evolved gain-of-function variant of the bee venom lytic peptide melittin identified in a high-throughput screen for small molecule leakage, enables the passage of macromolecules across bilayers under conditions where melittin and other pore-forming peptides do not. In surface-supported bilayers, MelP5 forms unusually high conductance, equilibrium pores at peptide:lipid ratios as low as 1:25000. The increase in bilayer conductance due to MelP5 is dramatically higher, per peptide, than the increase due to the parent sequence of melittin or other peptide pore formers. Here we also develop two novel assays for macromolecule leakage from vesicles, and we use them to characterize MelP5 pores in bilayers. We show that MelP5 allows the passage of macromolecules across vesicle membranes at peptide:lipid ratios as low as 1:500, and under conditions where neither osmotic lysis nor gross vesicle destabilization occur. The macromolecule-sized, equilibrium pores formed by MelP5 are unique as neither melittin nor other pore-forming peptides release macromolecules significantly under the same conditions. MelP5 thus appears to belong to a novel functional class of peptide that could form the foundation of multiple potential biotechnological applications.
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