摘要
Fluorescence spectroscopy was employed to investigate the interaction between fluorophore fluoresceinamine(FA) and bovine serum albumin(BSA) under physiological conditions. In the mechanism discussion, it was proved that the fluorescence quenching of BSA by FA is a result of the formation of a BSA-FA complex. Fluorescence quenching constants were determined using the modified Stern-Volmer equation to provide a measure of the binding affinity between FA and BSA. The results of the thermodynamic parameters △G, △H, and △S at different temperatures indicated that several kinds of interactions, except for the electrostatic interactions play cooperative roles in BSA-FA association. Furthermore, the conformation of BSA upon interaction with FA was also studied by synchrotron fluorescence spectroscopy.
Fluorescence spectroscopy was employed to investigate the interaction between fluorophore fluoresceinamine（FA） and bovine serum albumin（BSA） under physiological conditions. In the mechanism discussion, it was proved that the fluorescence quenching of BSA by FA is a result of the formation of a BSA-FA complex. Fluorescence quenching constants were determined using the modified Stern-Volmer equation to provide a measure of the binding affinity between FA and BSA. The results of the thermodynamic parameters △G, △H, and △S at different temperatures indicated that several kinds of interactions, except for the electrostatic interactions play cooperative roles in BSA-FA association. Furthermore, the conformation of BSA upon interaction with FA was also studied by synchrotron fluorescence spectroscopy.
基金
Supported by National Natural Science Foundation of China(Nos.21171086 and 81160213)
the Inner Mongolia Grassland Talent(No.108-108038)
the Inner Mongolia Autonomous Region Natural Science Foundation(No.2013MS1121)
the Inner Mongolia Agricultural University(Nos.211-109003 and 211-206038)
