Conformation and interaction of the cyclic cationic antimicrobial peptides in lipid bilayers
- 1 July 2002
- journal article
- research article
- Published by Wiley in Chemical Biology & Drug Design
- Vol. 60 (1) , 23-36
- https://doi.org/10.1034/j.1399-3011.2002.21003.x
Abstract
To investigate the role of peptide–membrane interactions in the biological activity of cyclic cationic peptides, the conformations and interactions of four membrane‐active antimicrobial pep...Keywords
This publication has 38 references indexed in Scilit:
- Membrane-bound structure and alignment of the antimicrobial β-sheet peptide gramicidin S derived from angular and distance constraints by solid state 19F-NMRJournal of Biomolecular NMR, 2001
- Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by α-helical antimicrobial and cell non-selective membrane-lytic peptidesBiochimica et Biophysica Acta (BBA) - Biomembranes, 1999
- Unusual β-sheet periodicity in small cyclic peptidesNature Structural & Molecular Biology, 1998
- Mode of action of linear amphipathic α-helical antimicrobial peptidesBiopolymers, 1998
- Nonlamellar Phases Induced by the Interaction of Gramicidin S with Lipid Bilayers. A Possible Relationship to Membrane-Disrupting ActivityBiochemistry, 1997
- Modulation of Structure and Antibacterial and Hemolytic Activity by Ring Size in Cyclic Gramicidin S AnalogsJournal of Biological Chemistry, 1996
- Gramicidin S is active against both gram‐positive and gram‐negative bacteriaInternational Journal of Peptide and Protein Research, 1996
- X-ray structure versus predicted conformation of Gramicidin SInternational Journal of Biological Macromolecules, 1980
- A conformational analysis of gramicidin S-A by nuclear magnetic resonance.Proceedings of the National Academy of Sciences, 1968
- Gramicidin S and its use in the Treatment of Infected WoundsNature, 1944