Clavanin A acetate is a peptide Antibiotic and membrane permeabilizer. Clavanin A acetate permeabilizes cytoplasmic membranes and unilamellar lipid bilayers, and dissipates membrane potential. Clavanin A acetate inserts into phospholipid monolayers via hydrophobic interactions under physiologically relevant surface pressures. Clavanin A acetate exhibits antibacterial activity against Micrococcus flavus. Clavanin A acetate can be used in studies related to Micrococcus flavus infection [1].
In Vitro, Clavanin A (starting serial dilution at 500 µg/mL; 24 h) acetate inhibits the growth of Micrococcus flavus (DSM 1790), with an MIC of 4.9 µM[1]. Clavanin A (0.23 µM) acetate dissipates the membrane potential of intact Micrococcus flavus cells, with inhibition rates reaching 58% and 80% at the concentration of 0.23 µM in two independent experiments[1]. Clavanin A (1-5 µM; 2 min) acetate permeabilizes DOPC large unilamellar vesicles (LUVs), triggering the release of low-molecular-weight carboxyfluorescein and high-molecular-weight FITC-dextran (9400 Da) in the micromolar concentration range, which indicates a non-specific membrane permeabilization mechanism[1].
References:
[1]. van Kan EJ, et al. Membrane activity of the peptide antibiotic clavanin and the importance of its glycine residues. Biochemistry. 2001;40(21):6398-6405.
In Vitro, Clavanin A (starting serial dilution at 500 µg/mL; 24 h) acetate inhibits the growth of Micrococcus flavus (DSM 1790), with an MIC of 4.9 µM[1]. Clavanin A (0.23 µM) acetate dissipates the membrane potential of intact Micrococcus flavus cells, with inhibition rates reaching 58% and 80% at the concentration of 0.23 µM in two independent experiments[1]. Clavanin A (1-5 µM; 2 min) acetate permeabilizes DOPC large unilamellar vesicles (LUVs), triggering the release of low-molecular-weight carboxyfluorescein and high-molecular-weight FITC-dextran (9400 Da) in the micromolar concentration range, which indicates a non-specific membrane permeabilization mechanism[1].
References:
[1]. van Kan EJ, et al. Membrane activity of the peptide antibiotic clavanin and the importance of its glycine residues. Biochemistry. 2001;40(21):6398-6405.