Membrane curvature stress and antibacterial activity of lactoferricin derivatives
| Autor: | Sylvie E. Blondelle, Dagmar Zweytick, Sabine Tumer, Karl Lohner |
|---|---|
| Rok vydání: | 2008 |
| Předmět: |
Membrane Fluidity
Surface Properties Molecular Conformation Biophysics Peptide Biology medicine.disease_cause Biochemistry Membrane Lipids chemistry.chemical_compound Lactoferricin Amphiphile Escherichia coli medicine Molecular Biology chemistry.chemical_classification Bilayer Cell Membrane Cell Biology Elasticity Anti-Bacterial Agents Lactoferrin Membrane chemistry Membrane curvature Stress Mechanical Antibacterial activity Antimicrobial Cationic Peptides |
| Zdroj: | Biochemical and Biophysical Research Communications. 369:395-400 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/j.bbrc.2008.01.176 |
| Popis: | We have studied correlation of non-lamellar phase formation and antimicrobial activity of two cationic amphipathic peptides, termed VS1-13 and VS1-24 derived from a fragment (LF11) of human lactoferricin on Escherichia coli total lipid extracts. Compared to LF11, VS1-13 exhibits minor, but VS1-24 significantly higher antimicrobial activity. X-ray experiments demonstrated that only VS1-24 decreased the onset of cubic phase formation of dispersions of E. coli lipid extracts, significantly, down to physiological relevant temperatures. Cubic structures were identified to belong to the space groups Pn3m and Im3m. Formation of latter is enhanced in the presence of VS1-24. Additionally, the presence of this peptide caused membrane thinning in the fluid phase, which may promote cubic phase formation. VS1-24 containing a larger hydrophobic volume at the N-terminus than its less active counterpart VS1-13 seems to increase curvature stress in the bilayer and alter the behaviour of the membrane significantly enhancing disruption. |
| Databáze: | OpenAIRE |
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