Interaction of ions and water in gramicidin A channels: streaming potentials across lipid bilayer membranes.
Open Access
- 1 September 1978
- journal article
- research article
- Published by Rockefeller University Press in The Journal of general physiology
- Vol. 72 (3), 327-340
- https://doi.org/10.1085/jgp.72.3.327
Abstract
For very narrow channels in which ions and water cannot overtake one another (single-file transport), electrokinetic measurements provide information about the number of water molecules within a channel. Gramicidin A is believed to form such narrow channels in lipid bilayer membranes. In 0.01 and 0.1 M solutions of CsCl, KCL, and NaCl, streaming potentials of 3.0 mV per osmolal osmotic pressure difference (created by urea, glycerol, or glucose) appear across gramicidin A-treated membranes. This implies that there are six to seven water molecules within a gramicidin channel. Electroosmotic experiments, in which the water flux assoicated with current flow across gramicidin-treated membranes is measured, corroborate this result. In 1 M salt solutions, streaming potentials are 2.35 mV per osmolal osmotic pressure difference instead of 3.0 mV. The smaller value may indicate multiple ion occupancy of the gramicidin channel at high salt concentrations. Apparent deviations from ideal cationic selectivity observed while attempting to measure single-salt dilution potentials across gramicidin-treated membranes result from streaming potential effects.This publication has 5 references indexed in Scilit:
- Water permeability of gramicidin A-treated lipid bilayer membranes.The Journal of general physiology, 1978
- Ionic selectivity, saturation, and block in gramicidin a channelsThe Journal of Membrane Biology, 1978
- Water and nonelectrolyte permeability of lipid bilayer membranes.The Journal of general physiology, 1976
- Effect of phloretin on the permeability of thin lipid membranes.The Journal of general physiology, 1976
- Structure of the K+ complex with nonactin, a macrotetrolide antibiotic possessing highly specific K+ transport propertiesJournal of Molecular Biology, 1967