ArticleScientific reports2017
Interaction of the Antimicrobial Peptide Aurein 1.2 and Charged Lipid Bilayer.
Article in Scientific reports, 2017. 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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Who cites it
18 citing papers in PubMed, 48 citations in OpenAlex.
- Self-assembling protein nanoparticles for cytosolic delivery of nucleic acids and proteins.Nature biotechnology · 2026Article
- Concentration Effects in Peptide-Lipid Bilayer Interactions: A Coarse-Grained Molecular Dynamics Study.The journal of physical chemistry. B · 2026Article
- Predicting peptide orientation in membrane interactions: a review on transmembrane and surface-bound states.European biophysics journal : EBJ · 2026Review
- Antimicrobial peptides: structure, functions and translational applications.Nature reviews. Microbiology · 2025Review
- Structure-Antimicrobial Activity Relationships of Recombinant Host Defence Peptides Against Drug-Resistant Bacteria.Microbial biotechnology · 2025Article
- Design, Synthesis, and Biological Evaluation of New Analogs of Aurein 1.2 Containing Non-Proteinogenic Amino Acids.Molecules (Basel, Switzerland) · 2025Article
- Charge, Hydrophobicity, and Lipid Type Drive Antimicrobial Peptides' Unique Perturbation Ensembles.Biochemistry · 2025Article
- A Critical Review of Short Antimicrobial Peptides from Scorpion Venoms, Their Physicochemical Attributes, and Potential for the Development of New Drugs.The Journal of membrane biology · 2024Review
- Antimicrobial Peptides: Challenging Journey to the Pharmaceutical, Biomedical, and Cosmeceutical Use.International journal of molecular sciences · 2023Review
- Small-Angle Neutron Scattering for Studying Lipid Bilayer Membranes.Biomolecules · 2022Review
- Harnessing the Role of Bacterial Plasma Membrane Modifications for the Development of Sustainable Membranotropic Phytotherapeutics.Membranes · 2022Review
- Interaction of a short antimicrobial peptide on charged lipid bilayer: A case study on aurein 1.2 peptide.BBA advances · 2022Article
- Antimicrobial Peptides and Their Applications in Biomedical Sector.Antibiotics (Basel, Switzerland) · 2021Review
- Aggregation and Its Influence on the Bioactivities of a Novel Antimicrobial Peptide, Temporin-PF, and Its Analogues.International journal of molecular sciences · 2021Article
- Intracellular delivery of therapeutic antibodies into specific cells using antibody-peptide fusions.Scientific reports · 2019Article
- Antimicrobial peptides: new hope in the war against multidrug resistance.Zoological research · 2019Review
- Alanine Scanning Studies of the Antimicrobial Peptide Aurein 1.2.Probiotics and antimicrobial proteins · 2019Article
- Could Cardiolipin Protect Membranes against the Action of Certain Antimicrobial Peptides? Aurein 1.2, a Case Study.ACS omega · 2018Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aurein 1.2 is a potent antimicrobial peptide secreted by frog Litoria aurea. As a short membrane-active peptide with only 13 amino acids in sequence, it has been found to be residing on the surface of lipid bilayer and permeabilizing bacterial membranes at high concentration. However, the detail at the molecular level is largely unknown. In this study, we investigated the action of Aurein 1.2 in charged lipid bilayers composed of DMPC/DMPG. Oriented Circular Dichroism results showed that the peptide was on the surface of lipid bilayer regardless of the charged lipid ratio. Only at a very high peptide-to-lipid ratio (~1/10), the peptide became perpendicular to the bilayer, however no pore was detected by neutron in-plane scattering. To further understand how it interacted with charged lipid bilayers, we employed Small Angle Neutron Scattering to probe lipid distribution across bilayer leaflets in lipid vesicles. The results showed that Aurein 1.2 interacted strongly with negatively charged DMPG, causing strong asymmetry in lipid bilayer. At high concentration, while the vesicles were intact, we found additional structure feature on the bilayer. Our study provides a glimpse into how Aurein 1.2 disturbs anionic lipid-containing membranes without pore formation.
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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.