Optimization of Microbial Specificity in Cyclic Peptides by Modulation of Hydrophobicity within a Defined Structural Framework
Open Access
- 1 January 2002
- journal article
- Published by Elsevier
- Vol. 277 (1), 67-74
- https://doi.org/10.1074/jbc.m107825200
Abstract
No abstract availableKeywords
This publication has 47 references indexed in Scilit:
- Development of the Structural Basis for Antimicrobial and Hemolytic Activities of Peptides Based on Gramicidin S and Design of Novel Analogs Using NMR SpectroscopyJournal of Biological Chemistry, 2000
- Insights into the mechanism of heterodimerization from the 1H-NMR solution structure of the c-Myc-Max heterodimeric leucine zipperJournal of Molecular Biology, 1998
- Cationic peptides: a new source of antibioticsTrends in Biotechnology, 1998
- Group additive contributions to the alcohol-induced α-helix formation of melittin: implication for the mechanism of the alcohol effects on proteinsJournal of Molecular Biology, 1998
- Animal antimicrobial peptides: An overviewBiopolymers, 1998
- Peptide Hydrophobicity Controls the Activity and Selectivity of Magainin 2 Amide in Interaction with MembranesBiochemistry, 1997
- Hydrophobic Effects on Antibacterial and Channel‐forming Properties of Cecropin A–Melittin HybridsJournal of Peptide Science, 1996
- Determination of disulphide bridges in PG‐2, an antimicrobial peptide from porcine leukocytesJournal of Peptide Science, 1995
- A Novel cDNA Sequence Encoding a Pig Leukocyte Antimicrobial Peptide with a Cathelin-like Pro-sequenceBiochemical and Biophysical Research Communications, 1993
- Environment‐dependent conformation and antimicrobial activity of a gramicidin S analog containing leucine and lysine residuesFEBS Letters, 1987