Valinomycin acts as a channel in ultrathin lipid membranes.
When the thickness of monolayer membranes formed by bolaform archaeal lipids is reduced to the approximate length of two valinomycin molecules, the zero-current conductance does not show any more a linear dependence on valinomycin concentration; instead, a quadratic behaviour is observed. This suggests that a dimer permeation pore is formed and therefore the conduction mechanism changes from carrier to channel.
Gliozzi
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Dipartimento di Fisica, Università di Genova, Genova, Italy. gliozzi@genova.infn.it
Robello
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M
Fittabile
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L
Relini
A
A
Gambacorta
A
A
D000473:Alkanes; D002725:Chloroform; D004075:Diglycerides / Q000737:chemistry / Q000378:metabolism; D004553:Electric Conductivity; D007473:Ion Channels; D008051:Lipid Bilayers / Q000378:metabolism; D008567:Membranes, Artificial; D014634:Valinomycin / Q000378:metabolism*
D000473:Alkanes; D004075:Diglycerides; D007473:Ion Channels; D008051:Lipid Bilayers; D008567:Membranes, Artificial; C085775:glycerol dialkyl nonitol tetraethyl ether; D014634:Valinomycin; D002725:Chloroform; C012867:decane