ArticleAnalytical chemistry2022
Measuring Thousands of Single-Vesicle Leakage Events Reveals the Mode of Action of Antimicrobial Peptides.
Article in Analytical chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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The trial behind it
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Who cites it
10 citing papers in PubMed.
- Prebiotic β-Strand Peptides May Be a Plausible Solution to the Protocell Permeability Problem.Journal of molecular evolution · 2026Review
- Systematic investigation of double emulsion dewetting dynamics for the robust production of giant unilamellar vesicles.Lab on a chip · 2026Article
- A robust method for on-chip production and manipulation of lipid vesicles by inverted emulsion.Cell reports methods · 2026Article
- Insect proteins and peptides: preparation, bioactivities, and applications.Food science of animal resources · 2026Article
- Molecular systems engineering of synthetic cells.Nature chemistry · 2026Review
- Giant unilamellar vesicles as a model system for studying ion transport.Biophysical reviews · 2025Review
- Strong Membrane Permeabilization Activity Can Reduce Selectivity of Cyclic Antimicrobial Peptides.The journal of physical chemistry. B · 2025Article
- Membrane-Active Peptides and Their Potential Biomedical Application.Pharmaceutics · 2023Review
- Article
- An ultrasensitive microfluidic approach reveals correlations between the physico-chemical and biological activity of experimental peptide antibiotics.Scientific reports · 2022Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Host defense or antimicrobial peptides hold promise for providing new pipelines of effective antimicrobial agents. Their activity quantified against model phospholipid membranes is fundamental to a detailed understanding of their structure-activity relationships. However, classical characterization assays often lack the ability to achieve this insight. Leveraging a highly parallelized microfluidic platform for trapping and studying thousands of giant unilamellar vesicles, we conducted quantitative long-term microscopy studies to monitor the membrane-disruptive activity of archetypal antimicrobial peptides with a high spatiotemporal resolution. We described the modes of action of these peptides via measurements of the disruption of the vesicle population under the conditions of continuous peptide dosing using a range of concentrations and related the observed modes to the molecular activity mechanisms of these peptides. The study offers an effective approach for characterizing membrane-targeting antimicrobial agents in a standardized manner and for assigning specific modes of action to the corresponding antimicrobial mechanisms.
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Registered trials
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