Photophysical Behavior and Fluorescence Quenching of l-Tryptophan in Choline Chloride-Based Deep Eutectic Solvents

Intrinsic fluorescence from l-tryptophan (l-Trp) is routinely used to obtain insight into the structural features and dynamics of proteins and enzymes. In contrast to aqueous enzymology, different parameters that control and influence the behavior of proteins and enzymes in nonaqueous media depend heavily on the solvent. Detailed analysis of the intrinsic fluorescence from l-Trp dissolved in two deep eutectic solvents (DESs), reline and glyceline, prepared by mixing salt choline chloride with H-bond donors urea and glycerol, respectively, in a 1:2 molar ratio within 298.15–358.15 K temperature range, is presented. Fluorescence emission maxima of l-Trp dissolved in DESs show bathochromic shift with increasing temperature. In comparison to water and several organic solvents, the fluorescence quantum yields of l-Trp in both DESs are significantly higher. While the rates of nonradiative decay in the two DESs are comparable and increase with increasing temperature, radiative decay rates are independent of temp...