title: Valinomycin acts as a channel in ultrathin lipid membranes.
abstract: 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.
authors.affiliation: Dipartimento di Fisica, Università di Genova, Genova, Italy. gliozzi@genova.infn.it
authors.forename: A
authors.initials: A
authors.lastname: Gliozzi
authors.forename: M
authors.initials: M
authors.lastname: Robello
authors.forename: L
authors.initials: L
authors.lastname: Fittabile
authors.forename: A
authors.initials: A
authors.lastname: Relini
authors.forename: A
authors.initials: A
authors.lastname: Gambacorta
mesh_terms: 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*
chemical_list: 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