The modulation of ion channels by the inhalation general anaesthetics. A1H-NMR investigation using unilamellar phospholipid membranes.
The modulation of a variety of mechanisms of channel-mediated transport across unilamellar phospholipid membranes by a range of halogenated inhalation general anaesthetics (chloroform, enflurane, halothane and methoxyflurane) was investigated using 1H-NMR spectroscopy. Transport of the probe ion Pr3+ across egg yolk phosphatidylcholine (PC) and dipalmitoyl phosphatidylcholine (DPPC) vesicular membranes in the presence of the channel forming polypeptides alamethicin 30 and melittin, and the polyene antibiotic nystatin, as well as the degree of vesicular lysis at the gel to liquid-crystal phase transition of DPPC vesicles was monitored. The observation that the inhalation general anaesthetics inhibit such membrane permeability independently of the channel system or type of lipid used, suggests that hydrogen-bonded water structure and/or hydrogen-bonding centres at dipolar lipid-polypeptide interfaces, can be likely sites of action of the general anaesthetics.
J A
JA
Veiro
G R
GR
Hunt
D000777:Anesthetics / Q000494:pharmacology*; D000001:Calcimycin; D004737:Enflurane / Q000494:pharmacology; D006221:Halothane / Q000494:pharmacology; D007473:Ion Channels / Q000187:drug effects* / Q000378:metabolism; D007700:Kinetics; D008081:Liposomes; D008555:Melitten; D008733:Methoxyflurane / Q000494:pharmacology; D008954:Models, Biological; D009761:Nystatin; D010713:Phosphatidylcholines; D011663:Pulmonary Surfactants
D000777:Anesthetics; D007473:Ion Channels; D008081:Liposomes; D010713:Phosphatidylcholines; D011663:Pulmonary Surfactants; D009761:Nystatin; D008555:Melitten; D008733:Methoxyflurane; D000001:Calcimycin; D004737:Enflurane; D006221:Halothane