Membrane aggregation and perturbation induced by antimicrobial peptide of S-thanatin
| Autor: | Xiaofang Li, Tao Xi, Xiaobo Fan, Jiaxuan Ding, Guoqiu Wu, Linxian Li, Zilong Shen, Hongbin Wu |
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| Rok vydání: | 2010 |
| Předmět: |
Biophysics
L Forms Peptide medicine.disease_cause Biochemistry Peptides Cyclic Membrane Potentials medicine Escherichia coli Molecular Biology chemistry.chemical_classification biology Vesicle Cell Membrane Cell Biology Periplasmic space biology.organism_classification Antimicrobial Fluoresceins Anti-Bacterial Agents Microscopy Electron Membrane chemistry Bacterial outer membrane Bacteria Antimicrobial Cationic Peptides Bacillus subtilis |
| Zdroj: | Biochemical and biophysical research communications. 395(1) |
| ISSN: | 1090-2104 |
| Popis: | Thanatin, a 21-residue peptide, is an inducible insect peptide. In our previous study, we have identified a novel thanatin analog of S-thanatin, which exhibited a broad antimicrobial activity against bacteria and fungi with low hemolytic activity. This study was aimed to delineate the antimicrobial mechanism of S-thanatin and identify its interaction with bacterial membranes. In this study, membrane phospholipid was found to be the target for S-thanatin. In the presence of vesicles, S-thanatin interestingly led to the aggregation of anionic vesicles and sonicated bacteria. Adding S-thanatin to Escherichia coli suspension would result in the collapse of membrane and kill bacteria. The sensitivity assay of protoplast elucidated the importance of outer membrane (OM) for S-thanatin's antimicrobial activity. Compared with other antimicrobial peptide, S-thanatin produced chaotic membrane morphology and cell debris in electron microscopic appearance. These results supported our hypothesis that S-thanatin bound to negatively charged LPS and anionic lipid, impeded membrane respiration, exhausted the intracellular potential, and released periplasmic material, which led to cell death. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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