Pulse fluorometry of cyclo-(glycyl-L-tryptophyl).
The fluorescence of cyclo-(glycyl-L-tryptophyl) in trimethyl phosphate has been studied in a temperature range varying from room temperature to -85 degrees C. At room temperature, the fluorescence decay is the sum of two exponentials, the relative amplitude of which depends on the emission wavelength. This can be explained by the presence of the two following emitting molecular states: on one hand the unfolded state, the fluorescence decay time and the emission spectrum of which are close to these of skatole; on the other hand the folded state which has a shorter decay time and a blue-shifted spectrum. By lowering the temperature, the fluorescence spectrum shifts to the blue, while the skatole spectrum shifts to the red. This behavior corresponds to an increase of the folded conformation concentration in agreement with the NMR results. Furthermore the rate of exchange between the folded and the unfolded conformations decreases. Accordingly the wavelength dependence of the fluorescence decay lessens. There are two possible values of the conformational angle x2 differing by 180 degrees, which correspond to the folded state; due to the indole asymmetry, the interactions between the indole and diketopiperazine rings differ in these conformers. Consequently the fluorescence decay remains biexponential even at -85 degrees C.
D004151:Dipeptides; D005998:Glycine; D008433:Mathematics; D008968:Molecular Conformation; D010456:Peptides, Cyclic; D011487:Protein Conformation; D013050:Spectrometry, Fluorescence; D013696:Temperature; D014364:Tryptophan
D004151:Dipeptides; D010456:Peptides, Cyclic; D014364:Tryptophan; D005998:Glycine