International Journal Of Chemistry, Mathematics And Physics(IJCMP)

Under simulated physiological conditions (pH=7.40), the interaction between Mobic and lysozyme was studied by synchronous fluorescence spectroscopy, ultraviolet spectroscopy, circular dichroism spectroscopy and molecular docking simulation technique.The results of spectroscopy showed that the fluorescence of lysozyme was statically quenched by Mobic, the number of binding sites was about 1, and the conformation of lysozyme was changed.The thermodynamic parameters obtained from the van't Hoff equation show that the Gibbs free energy ΔG<0 showed that the reaction between them was spontaneous, and ΔH<0, ΔS>0, indicating that the hydrophobic force plays an important role in the formation of Mobic-lysozyme complex.The results of molecular docking showed that the binding site of Mobic was close to the active site composed of Asp48 and Glu35 residues, indicating that Mobic could change the microenvironment of amino acid residues at the catalytic active center of lysozyme.The results of docking further showed that there was a hydrogen bond between Moby and lysozyme, so the interaction between Mobic and lysozyme was driven by hydrophobic interaction and hydrogen bond.