Binding study of diprophylline with lysozyme by spectroscopic methods

The binding properties of diprophylline (DPP) to lysozyme (Lys) were investigated using fluorescence spectroscopy in combination with UV–vis absorption techniques under simulative physiological conditions. Results of fluorescence measurement indicated that the intrinsic fluorescence of Lys was strongly quenched by DPP. The binding constants and the number of binding sites at different temperatures (298, 310, and 318 K) calculated with the data obtained from fluorescence quenching experiments via the modified Stern–Volmer equation were 8.61×104 L mol−1 and 1.34; 10.36×104 L mol−1 and 1.22; 12.85×104 L mol−1 and 1.11, respectively. Positive values of ΔH0 and ΔS0 obtained according to the Van’t Hoff equation for the formation of the DPP–Lys complex implied that typical hydrophobic interactions might play a significant role during the binding process. Furthermore, the effect of DPP on the conformation change of Lys was analyzed using synchronous fluorescence measurement. The effects of common co-ions on the interaction of DPP with Lys were also discussed.