Original Article
Qiu-Ju Zhang, Bao-Sheng Liu, G
Abstract
Gliquidone interacting with bovine serum albumin in physiological buffer (pH 7.4) was investigated by the fluorescence quenching spectroscopy and synchronous fluorescence spectroscopy. The analysis of the quenching mechanism was done using Stern–Volmer plots which exhibit upward (positive) deviation. The experimental results indicated that the quenching mechanism between bovine serum albumin and gliquidone was static, and the electrostatic interaction played an important role in the interaction. In addition, binding sites n, the apparent binding constant Ka, the thermodynamic parameters andHillÂÂ’s coefficients were calculated at different temperatures. The results obtained fromthe synchronous fluorescence were same with the results from the fluorescence quenching spectroscopy. In addition, synchronous fluorescence spectroscopy provided information about conformational changes of proteins.