Mast cell degranulating peptide forms voltage gated and cation-selective channels in lipid bilayers.
Mast cell degranulating peptide, a toxin of bee venom, is a polypeptide composed of 22 amino acids. Exposure of the asolectin bilayer to the peptide results in the formation of channels that are more permeable to K+ than Cl-. These channels are activated when the voltage of the cis side, to which the peptide is added, is made positive.
Ide
T
T
Department of Biophysical Engineering, Faculty of Engineering Science, Osaka University, Japan.
Taguchi
T
T
Morita
T
T
Sato
M
M
Ikenaka
K
K
Aimoto
S
S
Kondo
T
T
Hojo
H
H
Kasai
M
M
Mikoshiba
K
K
D001514:Bee Venoms / Q000032:analysis; D004553:Electric Conductivity; D066298:In Vitro Techniques; D007473:Ion Channels / Q000502:physiology*; D008051:Lipid Bilayers; D008407:Mast Cells / Q000502:physiology*; D008564:Membrane Potentials; D010455:Peptides / Q000502:physiology*; D010713:Phosphatidylcholines
D001514:Bee Venoms; D007473:Ion Channels; D008051:Lipid Bilayers; D010455:Peptides; D010713:Phosphatidylcholines; C008331:mast cell degranulating peptide