ArticleNanoscale2021
Membrane-selective nanoscale pores in liposomes by a synthetically evolved peptide: implications for triggered release.
Article in Nanoscale, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Engineering a single-chain immunoglobulin scaffold loaded with a latent-releasable cytotoxic pore-forming peptide.Communications biology · 2025Article
- D-M159 Synergistically Induces Apoptosis in HeLa Cells Through Endoplasmic Reticulum Stress and Mitochondrial Dysfunction.International journal of molecular sciences · 2025Article
- 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
- Interaction of Arginine-Rich Surfactant-like Peptide Nanotubes with Liposomes.Biomacromolecules · 2024Article
- Generation of a Nonbilayer Lipid Nanoenvironment after Epitope Binding Potentiates Neutralizing HIV-1 MPER Antibody.ACS applied materials & interfaces · 2024Article
- Structural Determinants of Peptide Nanopore Formation.ACS nano · 2024Article
- Novel non-helical antimicrobial peptides insert into and fuse lipid model membranes.Soft matter · 2024Article
- Enzymatically Triggered Peptide-Lipid Conjugation of Designed Membrane Active Peptides for Controlled Liposomal Release.ACS omega · 2024Article
- Leaky membrane fusion: an ambivalent effect induced by antimicrobial polycations.Nanoscale advances · 2022Article
- 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
- Peptide-Folding Triggered Phase Separation and Lipid Membrane Destabilization in Cholesterol-Rich Lipid Vesicles.Bioconjugate chemistry · 2022Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Peptides that form nanoscale pores in lipid bilayers have potential applications in triggered release, but only if their selectivity for target synthetic membranes over bystander biomembranes can be optimized. Previously, we identified a novel family of α-helical pore-forming peptides called "macrolittins", which release macromolecular cargoes from phosphatidylcholine (PC) liposomes at concentrations as low as 1 peptide per 1000 lipids. In this work, we show that macrolittins have no measurable cytolytic activity against multiple human cell types even at high peptide concentration. This unprecedented selectivity for PC liposomes over cell plasma membranes is explained, in part, by the sensitivity of macrolittin activity to physical chemical properties of the bilayer hydrocarbon core. In the presence of cells, macrolittins release all vesicle-entrapped cargoes (proteins and small molecule drugs) which are then readily uptaken by cells. Triggered release occurs without any direct effect of the peptide on the cells, and without vesicle-vesicle or vesicle-cell interactions.
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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.