title: Lysenin forms a voltage-dependent channel in artificial lipid bilayer membranes.
abstract: Lysenin, a hemolytic protein derived from the body fluid of earthworm, was incorporated into artificial bilayer membranes. Upon insertion, it formed a voltage-dependent large conductance channel in asolectin bilayers in a sphingomyelin-dependent manner. The channel had low ion-selectivity. Single-channel conductance was calculated as approximately 550 pS in 100 mM KCl. The channel in asolectin bilayers closed when the membrane was held at a positive potential. In contrast, the channel showed no voltage dependency in membranes made of pure phosphatidylcholine and sphingomyelin, suggesting some lipid contents included in the asolectin membranes affected channel gating.
authors.affiliation: Soft Biosystem Group, Laboratories for Nanobiology, Graduate School of Frontier Biosciences, Osaka University, Suita, Osaka 565-0871, Japan. ide@phys1.med.osaka-u.ac.jp
authors.forename: Toru
authors.initials: T
authors.lastname: Ide
authors.forename: Takaaki
authors.initials: T
authors.lastname: Aoki
authors.forename: Yuko
authors.initials: Y
authors.lastname: Takeuchi
authors.forename: Toshio
authors.initials: T
authors.lastname: Yanagida
mesh_terms: D000818:Animals; D007473:Ion Channels / Q000096:biosynthesis* / Q000502:physiology; D008051:Lipid Bilayers / Q000378:metabolism*; D010713:Phosphatidylcholines; D010743:Phospholipids; D011506:Proteins / Q000502:physiology*; D014118:Toxins, Biological
chemical_list: D007473:Ion Channels; D008051:Lipid Bilayers; D010713:Phosphatidylcholines; D010743:Phospholipids; D011506:Proteins; D014118:Toxins, Biological; C107040:lysenin; C024990:asolectin