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 ...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.展开更多
基金Project supported by the National Natural Science Foundation of China （No. 30370366）.
文摘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.
