Membrane permeability and antimicrobial kinetics of cecropin P1 against Escherichia coli

The interaction of cecropin P1 (CP1) with Escherichiacoli was investigated to gain insight into the time‐dependent antimicrobial action. Biophysical characterizations of CP1 with whole bacterial cells were performed using both fluorescent and colorimetric assays to investigate the role of membrane p...

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Veröffentlicht in:	Journal of peptide science 2009-06, Vol.15 (6), p.398-403
Hauptverfasser:	Arcidiacono, Steven, Soares, Jason W., Meehan, Alexa M., Marek, Patrick, Kirby, Romy
Format:	Artikel
Sprache:	eng
Schlagworte:	Anti-Infective Agents - chemistry Anti-Infective Agents - pharmacology antimicrobial activity antimicrobial peptide cecropin P1 Cell Membrane Permeability - drug effects Colorimetry E. coli Escherichia coli Escherichia coli - drug effects Escherichia coli - metabolism Kinetics lipopolysaccharide Lipopolysaccharides - chemistry membrane permeabilization Microbial Sensitivity Tests Peptides - chemistry Peptides - pharmacology Polymyxin B - chemistry Polymyxin B - pharmacology
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Zusammenfassung:	The interaction of cecropin P1 (CP1) with Escherichiacoli was investigated to gain insight into the time‐dependent antimicrobial action. Biophysical characterizations of CP1 with whole bacterial cells were performed using both fluorescent and colorimetric assays to investigate the role of membrane permeability and lipopolysaccharide (LPS) binding in lytic behavior. The kinetics of CP1 growth inhibition assays indicated a minimal inhibitory concentration (MIC) of 3 µM. Bactericidal kinetics at the MIC indicated rapid killing of E.coli (
ISSN:	1075-2617 1099-1387
DOI:	10.1002/psc.1125