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Channel formation kinetics of gramicidin A in lipid bilayer membranes

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Summary

Previous studies have given evidence that the active form of gramicidin A in lipid bilayer membranes is a dimer which acts as an ion channel; it has been further shown that the mean lifetime of the channel strongly depends on the membrane thickness. As the thickness slightly decreases when a voltage is applied to the membrane, the equilibrium between conducting dimers and nonconducting monomers may be displaced by a voltage jump. From the relaxation of the electrical current after the voltage jump, information about the kinetics of channel formation is obtained. For a dioleoyllecithin/n-decane membrane the rate constant of association is found to be 2×1014 cm2 mole−1 sec−1, which is by three orders of magnitude below the limiting value of a diffusion-controlled reaction in a two-dimensional system. The dissociation rate constant is equal to 2 sec−1, a value which is consistent with the channel lifetime as obtained from electrical fluctuation measurements.

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  1. Department of Biology, University of Konstanz, 7750, Konstanz, Germany

    E. Bamberg & P. Läuger

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  1. E. Bamberg
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  2. P. Läuger
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Bamberg, E., Läuger, P. Channel formation kinetics of gramicidin A in lipid bilayer membranes. J. Membrain Biol. 11, 177–194 (1973). https://doi.org/10.1007/BF01869820

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  • DOI: https://doi.org/10.1007/BF01869820

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