Interaction of primary amphipathic cell-penetrating peptides with phospholipid-supported monolayers
Copyright 2004 American Chemical Society
| Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1999. - 20(2004), 21 vom: 12. Okt., Seite 9255-61 |
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| 1. Verfasser: | |
| Weitere Verfasser: | , , , , , |
| Format: | Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2004
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| Zugriff auf das übergeordnete Werk: | Langmuir : the ACS journal of surfaces and colloids |
| Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Membranes, Artificial Peptides Phospholipids |
| Zusammenfassung: | Copyright 2004 American Chemical Society The mesoscopic organization adopted by two primary amphipathic peptides, P(beta) and P(alpha), in Langmuir-Blodgett (LB) films made of either the pure peptide or peptide-phospholipid mixtures was examined by atomic force microscopy. P(beta), a potent cell-penetrating peptide (CPP), and P(alpha) mainly differ by their conformational states, predominantly a beta-sheet for P(beta) and an alpha-helix for P(alpha), as determined by Fourier transform infrared spectroscopy. LB films of pure peptide, transferred significantly below their collapse pressure, were characterized by the presence of supramolecular structures, globular aggregates for P(beta) and filaments for P(alpha), inserted into the monomolecular film. In mixed peptide-phospholipid films, similar structures could be observed, as a function of the phospholipid headgroup and acyl chain saturation. They often coexisted with a liquid-expanded phase composed of miscible peptide-lipid. These data strongly suggest that primary amphipathic CPP and antimicrobial peptides may share, to some extent, common mechanisms of interaction with membranes |
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| Beschreibung: | Date Completed 25.04.2006 Date Revised 15.11.2006 published: Print Citation Status MEDLINE |
| ISSN: | 1520-5827 |