| Autor: |
W L Maloy, E. Krause, M. Bienert, D L MacDonald, M. Dathe, M. Beyermann |
| Rok vydání: |
2006 |
| Předmět: |
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| Zdroj: |
Peptide Science — Present and Future ISBN: 0792352718 |
| DOI: |
10.1007/0-306-46864-6_230 |
| Popis: |
Results and discussion Cationic, amphipathic, α-helical peptides are membrane active and able to disturb the barrier function of cell membranes [1, 2]. Some of the peptides possess antibacterial selectivity and are therefore of potential clinical relevance. Based on the hypothesis that the membrane activity is modulated by global structural features of the peptides [3] we investigated the role of hydrophobicity (H), the hydrophobic moment (μ) and the angle subtended by the hydrophobic helical face on the two steps of the membrane disturbing process: binding and membrane permeabilization. The peptide-induced effect on negatively charged phosphatdylglycerol (PG) and neutral phosphatidylcholine (PC) membranes was investigated using CD spectroscopy and fluorescence methods. The permeabilization of lipid vesicles was related to the antibacterial and hemolytic effect. Introduction |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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