Mechanism of Interaction Between Cefonicid Sodium and Trypsin by Spectroscopic and Molecular Docking Methods

The binding of cefonicid sodium (CFS) with trypsin was investigated by spectroscopic and molecular docking methods under different temperatures conditions (303, 310 and 318 K). The results demonstrated that the interaction between CFS and trypsin was taking place via static quenching with 1:1 binding ratio. The fluorescence datas were treated by using the double logarithmic equation, and the binding constants Ka of the interaction of CFS-trypsin systems and the number of binding sites n were obtained. The thermodynamic parameters of CFS-trypsin systems under different temperatures were obtained by the thermodynamic equation. The experimental data show that the interactions between them were mainly hydrophobic interaction and hydrogen bonding interaction, and with the molecular docking results are consistent.