ArticleJournal of the American Chemical Society2017
pH-Triggered, Macromolecule-Sized Poration of Lipid Bilayers by Synthetically Evolved Peptides.
Article in Journal of the American Chemical Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
34 citing papers in PubMed.
- The difference between MelP5 and melittin membrane poration.Scientific reports · 2025Article
- pH-Responsive Peptide Nanoparticles Deliver Macromolecules to Cells via Endosomal Membrane Nanoporation.ACS nano · 2024Article
- Enhancing the Intrinsic Antiplasmodial Activity and Improving the Stability and Selectivity of a Tunable Peptide Scaffold Derived from Human Platelet Factor 4.ACS infectious diseases · 2024Article
- Structural Determinants of Peptide Nanopore Formation.ACS nano · 2024Article
- Smart exosomes enhance PDAC targeted therapy.Journal of controlled release : official journal of the Controlled Release Society · 2024Article
- Cytosolic Delivery of Bioactive Cyclic Peptide Cargo by Spontaneous Membrane Translocating Peptides.ACS omega · 2024Article
- Plasma membrane damage limits cytoplasmic delivery by conventional cell penetrating peptides.PloS one · 2024Article
- The role of peptides in reversing chemoresistance of breast cancer: current facts and future prospects.Frontiers in pharmacology · 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
- New Technologies Bloom Together for Bettering Cancer Drug Conjugates.Pharmacological reviews · 2022Review
- Integrated Design of a Membrane-Lytic Peptide-Based Intravenous Nanotherapeutic Suppresses Triple-Negative Breast Cancer.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022Article
- Melittin-Based Nano-Delivery Systems for Cancer Therapy.Biomolecules · 2022Review
- Predicting Membrane-Active Peptide Dynamics in Fluidic Lipid Membranes.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Atomic force microscopy for quantitative understanding of peptide-induced lipid bilayer remodeling.Methods (San Diego, Calif.) · 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
- Unravelling cytosolic delivery of cell penetrating peptides with a quantitative endosomal escape assay.Nature communications · 2021Article
- Short oligoalanine helical peptides for supramolecular nanopore assembly and protein cytosolic delivery.RSC chemical biology · 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
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
pH-triggered membrane-permeabilizing peptides could be exploited in a variety of applications, such as to enable cargo release from endosomes for cellular delivery, or as cancer therapeutics that selectively permeabilize the plasma membranes of malignant cells. Such peptides would be especially useful if they could enable the movement of macromolecules across membranes, a rare property in membrane-permeabilizing peptides. Here we approach this goal by using an orthogonal high-throughput screen of an iterative peptide library to identify peptide sequences that have the following two properties: (i) little synthetic lipid membrane permeabilization at physiological pH 7 at high peptide concentration and (ii) efficient formation of macromolecule-sized defects in synthetic lipid membranes at acidic pH 5 and low peptide concentration. The peptides we selected are remarkably potent macromolecular sized pore-formers at pH 5, while having little or no activity at pH 7, as intended. The action of these peptides likely relies on tight coupling between membrane partitioning, α-helix formation, and electrostatic repulsions between acidic side chains, which collectively drive a sharp pH-triggered transition between inactive and active configurations with apparent pK
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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.