Spectroscopic study on the mechanism of meloxicam and α-amylase  

作　　者：Xu Cheng Baosheng Liu Hongcai Zhang 

机构地区：[1]College of Chemistry & Environmental Science, Key Laboratory of Analytical Science and Technology of Hebei Province, National Chemistry Experimental Teaching Demonstration Center, Hebei University, Baoding 071002, China

出　　处：《Journal of Pharmaceutical and Biopharmaceutical Research》2019年第1期28-35,共8页制药与生物制药研究杂志（英文）

摘　　要：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 -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 -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.

关 键 词：DRUG protein fluorescence analysis CONFORMATION molecular DOCKING BINDING rate 

分 类 号：R971.1[医药卫生—药品]