Modulation of Structure and Antibacterial and Hemolytic Activity by Ring Size in Cyclic Gramicidin S Analogs
Open Access
- 1 October 1996
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 271 (41) , 25261-25268
- https://doi.org/10.1074/jbc.271.41.25261
Abstract
No abstract availableKeywords
This publication has 43 references indexed in Scilit:
- Gramicidin S is active against both gram‐positive and gram‐negative bacteriaInternational Journal of Peptide and Protein Research, 1996
- Antimicrobial specificity and hemolytic activity of cyclized basic amphiphilic β-structural model peptides and their interactions with phospholipid bilayersBiochimica et Biophysica Acta (BBA) - Biomembranes, 1993
- Purification and characterization of a new metal protease which hydrolyzes the cyclic decapeptide, gramicidin SJournal of Fermentation and Bioengineering, 1993
- The Crisis in Antibiotic ResistanceScience, 1992
- Intermolecular anti-parallel β sheet: Comparison of predicted and observed conformations of gramicidin SProceedings of the National Academy of Sciences, 1980
- The crystal structure of a hydrated gramicidin S–urea complexNature, 1978
- Conformational states and biological activity of cyclic peptidesTetrahedron, 1975
- Enzymatic Hydrolysis of Gramicidin SThe Journal of Biochemistry, 1966
- Appendix 2—Possible molecular models for gramicidin S and their relationship to present ideas of protein structureBiochemical Journal, 1957
- Gramicidin S and its use in the Treatment of Infected WoundsNature, 1944