摘要
An optical biosensor with a stirred cuvette has been used to monitor the interaction between immobilized human serum albumin （HSA） and three water-soluble cationic porphyrins. The binding constants at 25℃ obtained from biosensor analysis were compared with those from fluorescence spectroscopy. The interactions were further investigated at temperatures from 15℃ to 30℃. The thermodynamics parameters, changes of free energy （△G）, enthalpy （△H） and entropy （△S）, were evaluated from equilibrium data. It appeared that the binding process was governed primarily by electrostatic forces.
An optical biosensor with a stirred cuvette has been used to monitor the interaction between immobilized human serum albumin （HSA） and three water-soluble cationic porphyrins. The binding constants at 25℃ obtained from biosensor analysis were compared with those from fluorescence spectroscopy. The interactions were further investigated at temperatures from 15℃ to 30℃. The thermodynamics parameters, changes of free energy （△G）, enthalpy （△H） and entropy （△S）, were evaluated from equilibrium data. It appeared that the binding process was governed primarily by electrostatic forces.
基金
Project supported by the National Natural Science Foundation of China （No. 30370366）.
