Antibacterial activity and pore-forming properties of ceratotoxins: a mechanism of action based on the barrel stave model
| Autor: | Nathalie Saint, Daniela Marchini, Gérard Molle, Yannick Bessin, Laura Marri |
|---|---|
| Rok vydání: | 2004 |
| Předmět: |
Fish Proteins
Erythrocytes Stereochemistry Lipid Bilayers Molecular Sequence Data Biophysics Biochemistry Ion Channels Protein Structure Secondary Hemolysin Proteins Amphiphile medicine Animals Humans alpha-helical peptide Molecule Amino Acid Sequence Lipid bilayer Ion channel α-helical peptide Chemistry ion channel lipid bilayer conductance Electric Conductivity Cationic polymerization Proteins Ceratitis capitata Cell Biology Anti-Bacterial Agents Protein Structure Tertiary Membrane Models Chemical Mechanism of action Insect Proteins medicine.symptom Antibacterial activity |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Biomembranes. 1667:148-156 |
| ISSN: | 0005-2736 |
| DOI: | 10.1016/j.bbamem.2004.09.011 |
| Popis: | Ceratotoxins are α-helical cationic peptides isolated from the medfly Ceratitis capitata. These amphipathic peptides were found to display strong antibacterial activity and weak hemolytic activity. When reconstituted into planar lipid bilayers, ceratotoxins developed highly asymmetric I/V curves under voltage ramps and formed, in single-channel experiments, well-defined voltage-dependent ion channels according to the barrel stave model. The antibacterial activity and pore-forming properties of these molecules were well correlated. Similar experiments performed with synthesized truncated fragments showed that the C-terminal domain of ceratotoxins is strongly implicated in the formation of helical bundles in the membrane whereas the largely cationic N-terminal region is likely to anchor ceratotoxins on the lipid surface. |
| Databáze: | OpenAIRE |
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