Study on the Features of the Binding Reaction Between Pefloxacin and Bovine Serum Albumin Using Fluorescence Spectrophotometry

Under different temperatures, the binding of pefloxacin to bovine serum albumin (BSA) was studied by means of the fluorescence quenching spectrum, the synchronous fluorescence spectrum, the three-dimensional fluorescence spectrum, and the ultra-violet spectrum. After analyzing the fluorescence quenching data using the Stern-Volmer equation, the Lineweaver-Burk equation and the thermodynamic equation, the average value of the bonding constant (KLB: 8.419 × 103 M), the thermodynamic parameters (ΔHθ:150.7 KJ mol−1, ΔGθ:−22.88 KJ mol−1, ΔSθθ:561.9 J K−1), and the number of bonding sites (1.081) were obtained. It has been proved that pefloxacin and BSA can react with each other and form a new compound under different experimental concentrations and temperatures, with the fluorescence quenching being static and the force being of hydrophobic force. It provides important information for studying the pharmacological effects and the biological effects of pefloxacin and the configuration changes caused by pefloxacin in proteins.