| Autor: |
Sabine Tumer, Dagmar Zweytick, Roman Jerala, Guillermo Martinez de Tejada, Sylvie E. Blondelle, Guenter Deutsch, Daniel Monreal, Karl Lohner, Mateja Zorko |
| Rok vydání: |
2009 |
| Předmět: |
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| Zdroj: |
Biophysical Journal. 96(3) |
| ISSN: |
0006-3495 |
| DOI: |
10.1016/j.bpj.2008.12.697 |
| Popis: |
The effect of short peptides, derived from lactoferricin, a human host defense peptide exhibiting antibacterial activity and their N-acylated derivatives was studied with biological and membrane mimetic systems. The work carried out during the European RTD-Project “ANEPID” revealed correlation between biological activity against E.coli and interaction with negatively charged lipid model systems, leading to formation of peptide effected lipid domains. Increase of hydrophobicity by addition of hydrophobic amino acids as well as N-acylation improved activity in model and biological systems, but was limited by loss of selectivity for bacterial systems. Addition of peptides to bacterial mimics caused de-mixing into charged peptide effected domains and neutral mainly unaffected domains. Following induction of membrane curvature stress and leakage of cellular contents at defect lines of these induced domains appear to be the major effects of the studied peptides, which could be proven with E.coli mimetic systems. Major perturbance of cytoplasmic membranes of bacteria was also revealed by electron microscopy indicated by peptide induced formation of large membrane blebs and partially by detection of oversized cells that might reflect peptide induced defects in cell-division. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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