Related Experiment Video
Updated: Aug 25, 2026

Production and Visualization of Bacterial Spheroplasts and Protoplasts to Characterize Antimicrobial Peptide Localization
Published on: August 11, 2018
The antibacterial peptide ceratotoxin A displays alamethicin-like behavior in lipid bilayers
Nathalie Saint1, Laura Marri, Daniela Marchini
1CBS, UMR 5048 CNRS, UMR 554 INSERM, Université de Montpellier 1, 29 rue de Navacelles, 34090 Montpellier, France.
Abstract:
Ceratotoxin A (CtxA), a 36-residue alpha-helical cationic peptide isolated from the medfly Ceratitis capitata, exhibits strong antibacterial activity. To determine its mode of action against bacteria, we investigated the behavior of ceratotoxin A by incorporating it into planar lipid bilayers. Macroscopic and single channel conductance experiments showed that ceratotoxin A forms voltage-dependent ion channels in bilayers according to the barrel-stave model. The characteristics of the channel suggest that the C-terminal regions form bundles of five or six helices embedded in the membrane, such that the N-terminal moieties lie on the polar side of the lipid bilayer.
More Related Videos
Related Concept Videos
Inhibitors of Gram-positive Cell Wall Synthesis
Inhibitors of Bacterial Protein Synthesis
Bacterial Toxins
Cytoskeletal Proteins in Bacteria
Detergent Purification of Membrane Proteins
Antifungal Agents

