Effect of temperature on the interaction of gramicidin A and its dimer analog with the muscle fiber membrane

Potassium conductance of single muscle fibres from Rana esculenta was studied in isotonic K2SO4 solution under constant current conditions using double sucrose gap method. At room temperature the channel formation by gramicidin was much faster than that of the synthetic head to head covalently linked gramicidin dimer. The increase of temperature by 8-10 degrees C resulted in a considerable rise of both dimer- and gramicidin-induced conductances. The effect was much greater than in the case of bilayers indicating a remarkable entropy change in the muscle fibre membrane. The temperature dependence of adsorption was more pronounced than that of desorption: there was no effect on desorption of dimer and only 20% of the temperature-activated desorption of gramicidin irreversibly bound at room temperature.