ArticleScientific reports2015
Controls and constrains of the membrane disrupting action of Aurein 1.2.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 71 citations in OpenAlex.
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- The Role of Flexibility in the Bioactivity of Short α-Helical Antimicrobial Peptides.Antibiotics (Basel, Switzerland) · 2025Review
- Mechanistic insights into endosomal escape by sodium oleate-modified liposomes.Beilstein journal of nanotechnology · 2024Article
- Antibacterial Activity and Mechanisms of TroHepc2-22, a Derived Peptide of Hepcidin2 from Golden Pompano (International journal of molecular sciences · 2023Article
- Structurally Modified Bioactive Peptide Inhibits SARS-CoV-2 Lentiviral Particles Expression.Pharmaceutics · 2022Article
- New Antimicrobial Peptide with Two CRAC Motifs: Activity againstMicroorganisms · 2022Article
- The Influence of Short Motifs on the Anticancer Activity of HB43 Peptide.Pharmaceutics · 2022Article
- Rationales Design von Phe-BODIPY-Aminosäuren als fluorogene Bausteine für den peptidbasierten Nachweis vonAngewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2022Article
- Rational Design of Phe-BODIPY Amino Acids as Fluorogenic Building Blocks for Peptide-Based Detection of Urinary Tract Candida Infections.Angewandte Chemie (International ed. in English) · 2022Article
- Interaction of a short antimicrobial peptide on charged lipid bilayer: A case study on aurein 1.2 peptide.BBA advances · 2022Article
- A reversible cell penetrating peptide-cargo linkage allows dissection of cell penetrating peptide- and cargo-dependent effects on internalization and identifies new functionalities of putative endolytic peptides.Frontiers in pharmacology · 2022Article
- Design, Synthesis and Antifungal Activity of Stapled Aurein1.2 Peptides.Antibiotics (Basel, Switzerland) · 2021Article
- Latest developments on the mechanism of action of membrane disrupting peptides.Biophysics reports · 2021Article
- Marine Invertebrate Peptides: Antimicrobial Peptides.Frontiers in microbiology · 2021Review
- A Novel Antimicrobial Peptides From Pine Needles ofFrontiers in microbiology · 2021Article
- Improved Stability and Activity of a Marine Peptide-N6NH2 againstMarine drugs · 2020Article
- Interaction of Silver-Lignin Nanoparticles With Mammalian Mimetic Membranes.Frontiers in bioengineering and biotechnology · 2020Article
- Inhibition of K-Ras4B-plasma membrane association with a membrane microdomain-targeting peptide.Chemical science · 2019Article
- Alanine Scanning Studies of the Antimicrobial Peptide Aurein 1.2.Probiotics and antimicrobial proteins · 2019Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aurein 1.2 is a 13 residue antimicrobial peptide secreted by the Australian tree frog Litoria Aurea. It is a surface-acting membrane disrupting peptide that permeabilizes bacterial membranes via the carpet mechanism; the molecular details of this process are mostly unknown. Here the mechanism of action of Aurein 1.2 was investigated with an emphasis on the role of membrane charge and C-terminal amidation of the peptide. Using quartz crystal microbalance (QCM) fingerprinting it was found that the membrane charge correlates with membrane affinity of the peptide, however the binding and the membrane disrupting processes are not charge driven; increased membrane charge reduces the membrane disrupting activity. Coarse grain simulations revealed that phenylalanine residues act as membrane anchors. Accordingly Aurein 1.2 has the ability to bind to any membrane. Furthermore, bundling precludes membrane disruption in case of wild type peptides, while non C-terminal amidated peptides form random aggregates leading to detachment from the membrane. Hence C-terminal amidation is crucial for Aurein 1.2 action. Our results suggest that Aurein 1.2 acts via aggregation driven membrane penetration. The concomitant change in the tension of the outer leaflet imposes a spontaneous curvature on the membrane, leading to disintegration.
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