Synchronous fluorescence and molecular docking to explore the mechanism of meloxicam and lipase
Xu Cheng, Baosheng Liu, Hongcai Zhang
The interaction between lipase and rheumatoid arthritis drug meloxicam (MEL)were studied by synchronous fluorescence method under pH=7.40. The results showed that MEL quenched the fluorescence of Tyr residues and Trp residues in a static quenching manner. Fluorescence quenching ratio showed that the binding position was closer to the Trp residue. The binding rate of MEL to Tyr residue in lipase was W(Q)=1.10%~0.77%, W(B)=1.10%~30.96%, and the binding rate to Trp residue W(Q)= 1.64%~1.01%, W(B)= 1.64%~40.23%, respectively, the binding model was established. The main types of MEL and lipase binding system are hydrophobic interaction and hydrogen bonding, and there is no synergistic effect in the binding. The molecular docking results indicate that the optimal binding position is near the active center of lipase, and the combination of the two changes. In the microenvironment at the active center, the combined reaction may have an effect on the digestion of fatty substances.