Open Access Peer-reviewed Research Article

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Xu Cheng
Baosheng Liu corresponding author
Hongcai Zhang


In order to explore the mechanism of action of meloxicam and α-amylase. The interaction between the rheumatoid arthritis drug meloxicam and α-amylase was studied by fluorescence spectroscopy, synchronous fluorescence spectroscopy and molecular docking under the experimental conditions of pH=6.80. The results showed that meloxicam was able to effectively quench the endogenous fluorescence of α-amylase in a static quenching form a 1:1 complex and change the conformation of α-amylase. Thermodynamic results indicated that the main type of meloxicam and α-amylase system was hydrophobic interaction. Molecular docking indicated that the binding system had hydrogen bonds in addition to hydrophobic interaction and meloxicam was surrounded by the active amino acid residues Trp13 and Trp263 of α-amylase, which changed the microenvironment of amino acid residues at the active center of α-amylase. By establishing the binding model, it can be seen that the protein binding rate W(B) of meloxicam to α-amylase was 2.76%-41.79% under the experimental conditions. The results showed that the binding of meloxicam to α-amylase had an effect on the number of free α-amylase. The drug binding rate W(Q) of the system was 2.76%-1.67%, which indicated that the combination of α-amylase and meloxicam would not affect the efficacy of meloxicam.

protein, fluorescence analysis, conformation, molecular docking, binding rate

Article Details

How to Cite
Cheng, X., Liu, B., & Zhang, H. (2019). Spectroscopic study on the mechanism of meloxicam and α-amylase. Journal of Pharmaceutical and Biopharmaceutical Research, 1(1), 28-35.


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