title: Asymmetry of syringomycin E channel studied by polymer partitioning.
abstract: To probe the size of the ion channel formed by Pseudomonas syringae lipodepsipeptide syringomycin E, we use the partial blockage of ion current by penetrating poly(ethylene glycol)s. Earlier experiments with symmetric application of these polymers yielded a radius estimate of approximately 1 nm. Now, motivated by the asymmetric non-ohmic current-voltage curves reported for this channel, we explore its structural asymmetry. We gauge this asymmetry by studying the channel conductance after one-sided addition of differently sized poly(ethylene glycol)s. We find that small polymers added to the cis-side of the membrane (the side of lipodepsipeptide addition) reduce channel conductance much less than do the same polymers added to the trans-side. We interpret our results to suggest that the water-filled pore of the channel is conical with cis- and trans-radii differing by a factor of 2-3 and that the smaller cis-radius is in the 0.25-0.35 nm range. In symmetric, two-sided addition, polymers entering the pore from the larger opening dominate blockage.
authors.affiliation: Institute of Cytology of the Russian Academy of Sciences, St. Petersburg, 194064, Russia.
authors.forename: Olga S
authors.initials: OS
authors.lastname: Ostroumova
authors.forename: Philip A
authors.initials: PA
authors.lastname: Gurnev
authors.forename: Ludmila V
authors.initials: LV
authors.lastname: Schagina
authors.forename: Sergey M
authors.initials: SM
authors.lastname: Bezrukov
mesh_terms: D007473:Ion Channels / Q000737:chemistry / Q000378:metabolism*; D008051:Lipid Bilayers / Q000737:chemistry / Q000378:metabolism; D008954:Models, Biological; D010456:Peptides, Cyclic / Q000737:chemistry / Q000378:metabolism*; D011092:Polyethylene Glycols; D044224:Pseudomonas syringae / Q000378:metabolism
chemical_list: D007473:Ion Channels; D008051:Lipid Bilayers; D010456:Peptides, Cyclic; C105246:syringomycin E; D011092:Polyethylene Glycols