Thermodynamic studies on the interaction of dioxopromethazine to beta-cyclodextrin and bovine serum albumin.

The interaction of dioxopromethazine (DOPM) with beta-cyclodextrin (beta-CD) and bovine serum albumin (BSA) were investigated by fluorescence quenching method. It was shown that DOPM has quite a strong ability to quench the fluorescence launching from BSA by reacting with it and forming a certain kind of new compound. The quenching and the energy transfer mechanisms were discussed, respectively. The binding constants and thermodynamic parameters at four different temperatures, the binding locality, and the binding power were obtained. The conformation of BSA was discussed by synchronous and three-dimensional fluorescence techniques. The inclusion reaction between beta-CD and DOPM was explored by both Lineweaver-Burk equation and Benesi-Hildebrand equation. The inclusion constants and the thermodynamic parameters at 297 and 307 K were figured out, respectively. The mechanism of inclusion reaction was speculated and the slow release characteristics of beta-CD to DOPM was attempted to explain at molecule level.