Bilayer Interactions of Indolicidin, a Small Antimicrobial Peptide Rich in Tryptophan, Proline, and Basic Amino Acids
- 1 February 1997
- journal article
- Published by Elsevier in Biophysical Journal
- Vol. 72 (2), 794-805
- https://doi.org/10.1016/s0006-3495(97)78713-7
Abstract
No abstract availableKeywords
This publication has 37 references indexed in Scilit:
- Binding of small basic peptides to membranes containing acidic lipids: theoretical models and experimental resultsBiophysical Journal, 1996
- Mode of Action of the Antimicrobial Peptide IndolicidinJournal of Biological Chemistry, 1996
- Interactions Contributing to the Formation of a β-Hairpin-like Structure in a Small PeptideBiochemistry, 1996
- Control of topology and mode of assembly of a polytopic membrane protein by positively charged residuesNature, 1989
- Vesicles of variable sizes produced by a rapid extrusion procedureBiochimica et Biophysica Acta (BBA) - Biomembranes, 1986
- Incorporation of Melittin into phosphatidylcholine bilayersFEBS Letters, 1981
- Determination of protein secondary structure in solution by vacuum ultraviolet circular dichroismJournal of Molecular Biology, 1980
- Intrinsic fluorescence study of lipid-protein interactions in membrane models. Binding of melittin, an amphipathic peptide, to phospholipid vesiclesBiochimica et Biophysica Acta (BBA) - Biomembranes, 1977
- The calculated circular dichroism of polyproline ii in the polarizability approximationBiopolymers, 1974
- Interaction of alytic polypeptide, melittin, with lipid membrane systems.1969