ArticleEuropean biophysics journal : EBJ2014
Dye-release assay for investigation of antimicrobial peptide activity in a competitive lipid environment.
Article in European biophysics journal : EBJ, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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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
18 citing papers in PubMed, 49 citations in OpenAlex.
- Membrane interactions and pore stability of aurein 1.2 and LLAA in single- and multi-peptide systems revealed by coarse-grained molecular dynamics simulations.Journal of molecular modeling · 2026Article
- Investigating How Lysophosphatidylcholine and Lysophosphatidylethanolamine Enhance the Membrane Permeabilization Efficacy of Host Defense Peptide Piscidin 1.The journal of physical chemistry. B · 2025Article
- Host-defense piscidin peptides as antibiotic adjuvants against Clostridioides difficile.PloS one · 2024Article
- Antiviral activity of the host defense peptide piscidin 1: investigating a membrane-mediated mode of action.Frontiers in chemistry · 2024Article
- Article
- The membrane activity of the antimicrobial peptide caerin 1.1 is pH dependent.Biophysical journal · 2023Article
- An Antimicrobial Peptide-Mimetic Methacrylate Random Copolymer Induces Domain Formation in a Model Bacterial Membrane.The Journal of membrane biology · 2022Review
- C-terminus amidation influences biological activity and membrane interaction of maculatin 1.1.Amino acids · 2021Article
- Interaction of synthetic antimicrobial peptides of the Hylin a1 family with models of eukaryotic structures: Zwitterionic membranes and DNA.Biochemistry and biophysics reports · 2020Article
- In-cell Solid-State NMR Studies of Antimicrobial Peptides.Frontiers in medical technology · 2020Review
- The Location of the Antimicrobial Peptide Maculatin 1.1 in Model Bacterial Membranes.Frontiers in chemistry · 2020Article
- Mode-of-Action of Antimicrobial Peptides: Membrane Disruption vs. Intracellular Mechanisms.Frontiers in medical technology · 2020Review
- In Situ Monitoring of Bacteria under Antimicrobial Stress UsingInternational journal of molecular sciences · 2019Article
- Could Cardiolipin Protect Membranes against the Action of Certain Antimicrobial Peptides? Aurein 1.2, a Case Study.ACS omega · 2018Article
- One pathogen two stones: are Australian tree frog antimicrobial peptides synergistic against human pathogens?European biophysics journal : EBJ · 2017Article
- Investigating the Interaction of Octapeptin A3 with Model Bacterial Membranes.ACS infectious diseases · 2017Article
- Controls and constrains of the membrane disrupting action of Aurein 1.2.Scientific reports · 2015Article
- Bacteria May Cope Differently from Similar Membrane Damage Caused by the Australian Tree Frog Antimicrobial Peptide Maculatin 1.1.The Journal of biological chemistry · 2015Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A dye-release method for investigating the effect of a competitive lipid environment on the activity of two membrane-disrupting antimicrobial peptides (AMP), maculatin 1.1 and aurein 1.2, is presented. The results support the general conclusion that AMP have greater affinity for negatively charged membranes, for example bacterial membranes, than for the neutral membrane surface found in eukaryotic cells, but only within a competitive lipid environment. Indeed, in a single-model membrane environment, both peptides were more potent against neutral vesicles than against charged vesicles. The approach was also used to investigate the effect of pre-incubating the peptides in a neutral lipid environment then introducing charged lipid vesicles. Maculatin was shown to migrate from the neutral lipid bilayers, where pores had already formed, to the charged membrane bilayers. This result was also observed for charged-to-charged bilayers but, interestingly, not for neutral-to-neutral lipid interfaces. Aurein was able to migrate from either lipid environment, indicating weaker binding to lipid membranes, and a different molecular mechanism for lysis of lipid bilayers. Competitive lipid environments could be used to assess other critical conditions that modulate the activity of membrane peptides or proteins.
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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.