Mode of action of gramicidin S on Escherichia coli membrane.
The action of a cationic antibiotic gramicidin S on the outer and cytoplasmic membranes of Escherichia coli was studied. It was found that gramicidin S disrupted the permeability barrier of the outer membrane, permitting the permeation of an antibiotic ionophore, this being similar to the action of the dimer in compound 48/80 (Katsu, T., Shibata, M. and Fujita, Y. (1985) Biochim. Biophys. Acta 818, 61-66). However, differently from the dimer, gramicidin S further stimulated the efflux of K+ through the cytoplasmic membrane of E. coli. The time course of K+ permeability change accorded well with that of change in the viability of E. coli cells. These changes occurred at temperatures above the phase transition of the cytoplasmic membrane. This temperature range differed greatly from the case of polymyxin B, a polycationic antibiotic acting at temperatures above the phase transition of the outer membrane. We discuss the mode of gramicidin S action on the cytoplasmic membrane of E. coli, in comparison with the results on red blood cells and liposomes.
D002462:Cell Membrane / Q000187:drug effects* / Q000648:ultrastructure; D002463:Cell Membrane Permeability / Q000187:drug effects; D004910:Erythrocyte Membrane / Q000187:drug effects; D004926:Escherichia coli / Q000187:drug effects* / Q000648:ultrastructure; D006096:Gramicidin / Q000494:pharmacology*; D008081:Liposomes; D011112:Polymyxin B / Q000494:pharmacology; D011188:Potassium / Q000378:metabolism; D013696:Temperature; D003189:p-Methoxy-N-methylphenethylamine / Q000494:pharmacology
D008081:Liposomes; D006096:Gramicidin; D003189:p-Methoxy-N-methylphenethylamine; D011112:Polymyxin B; D011188:Potassium