Open AccessThe mechanism of action of chlorhexidine
Author(s) -
Kuyyakad Thicumporn,
Quesnel Louis B.
Publication year - 1992
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1992.tb14042.x
Subject(s) - chlorhexidine , chemistry , dinitrophenol , polymyxin , atpase , mechanism of action , escherichia coli , atp hydrolysis , polymyxin b , biochemistry , microbiology and biotechnology , biology , enzyme , antibiotics , in vitro , medicine , dentistry , gene
Chlorhexidine did not inhibit ATPase in intact cells of Escherichia coli K12 W1317i − , even at bactericidal concentrations, and ATP hydrolysis was greatest at the highest concentration (40 mg/l), even though no net uptake of substrate occurred. Like dinitrophenol and tribrominated salicylanilide, polymyxin and chlorhexidine collapsed the membrane potential at inhibitory concentrations. Membrane disruption, and not ATPase inactivation, is considered the lethal event in chlorhexidine action.