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Biophysical Journal 61: 1306-1315 (1992)
© 1992 the Biophysical Society

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Influence of ion occupancy and membrane deformation on gramicidin A channel stability in lipid membranes.

A Ring

Department of Physiology and Medical Biophysics, Biomedical Centre, Uppsala, Sweden.

ABSTRACT

The average lifetime of gramicidin A channels in monoolein/decane bilayer membranes was measured. The results support the hypothesis of channel stabilization by ion occupancy. The effects of electric field and salt concentration are consistent with the expected effects on both occupancy and membrane compression. The lifetime in asymmetric solutions with divalent cation blockers on one side of the membrane shows a voltage dependence such that the lifetime decreases for positive voltages applied from the blocking side and increases for negative voltages. This result strongly supports the occupancy hypothesis. The lifetime increases with permeant ion concentration, and at the one molar level it also increases with voltage. The voltage dependence of lifetime for a low concentration of permeant ion depends on the total salt level. The results for these conditions are consistent with the assumption that membrane compression also influences the lifetime, even for the "soft" solvent-containing membrane considered here. It is proposed that the channel nearest neighbor lipids need not be fixed in a plane at the channel end. Using a liquid crystal model it may then be shown that surface tension is the major component of the membrane deformation free energy, which may explain the significant effects of the membrane compression on the lifetime.




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T. K. Rostovtseva, H. I. Petrache, N. Kazemi, E. Hassanzadeh, and S. M. Bezrukov
Interfacial Polar Interactions Affect Gramicidin Channel Kinetics
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G. V. Miloshevsky and P. C. Jordan
Gating Gramicidin Channels in Lipid Bilayers: Reaction Coordinates and the Mechanism of Dissociation
Biophys. J., January 1, 2004; 86(1): 92 - 104.
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Copyright © 1992 by the Biophysical Society.