Tryptophan photolysis is responsible for gramicidin-channel inactivation by ultraviolet light.
The decay of gramicidin fluorescence resulting from ultraviolet exposure was compared to the decay of conductance from gramicidin-containing planar bilayer membranes under the same conditions of illumination. The decay rate was the same for both processes. The fluorescence decay was identical whether gramicidin was dissolved in methanol or incorporated into lipid vesicles, indicating that the peptide conformation does not affect the sensitivity of gramicidin to photolysis. The correlation of fluorescence decay and conductance decay imply that conductance loss from gramicidin-doped membranes illuminated with ultraviolet light is due to photochemical modifications of the channel tryptophans rather than simply to disturbance of the conformation of gramicidin channels.
D006096:Gramicidin / Q000378:metabolism*; D007473:Ion Channels / Q000528:radiation effects*; D008564:Membrane Potentials; D000432:Methanol; D010782:Photolysis; D011487:Protein Conformation; D014364:Tryptophan / Q000494:pharmacology*; D014466:Ultraviolet Rays
D007473:Ion Channels; D006096:Gramicidin; D014364:Tryptophan; D000432:Methanol