Lysenin forms a voltage-dependent channel in artificial lipid bilayer membranes.
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.
Ide
Toru
T
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
Aoki
Takaaki
T
Takeuchi
Yuko
Y
Yanagida
Toshio
T
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
D007473:Ion Channels; D008051:Lipid Bilayers; D010713:Phosphatidylcholines; D010743:Phospholipids; D011506:Proteins; D014118:Toxins, Biological; C107040:lysenin; C024990:asolectin