Spectroscopic study and application of the interaction mechanism of meloxicam with trypsin

In order to explore the interaction between meloxicam and trypsin, the interaction mechanism between meloxicam and trypsin was studied by fluorescence spectrum, UV-vis absorption spectrum, circular dichroism spectrum, and molecular docking simulation under the experimental condition of pH = 7.40. Th...

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Bibliographic Details
Published in:Spectroscopy letters 2019-07, Vol.52 (6), p.321-329
Main Authors: Liu, Bao-Sheng, Cheng, Xu, Zhang, Hong-Cai, Ma, Li-Hua, Wang, Chun-Dan
Format: Article
Language:English
Subjects:
Absorption spectra
binding rate
Binding sites
Catalysis
Chemical bonds
Computer simulation
Dichroism
Fluorescence
Hydrogen bonding
Hydrophobicity
meloxicam
Molecular docking
Proteins
spectroscopy
Trypsin
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Summary:In order to explore the interaction between meloxicam and trypsin, the interaction mechanism between meloxicam and trypsin was studied by fluorescence spectrum, UV-vis absorption spectrum, circular dichroism spectrum, and molecular docking simulation under the experimental condition of pH = 7.40. The results of spectral experiments showed that meloxicam could effectively quench the internal fluorescence of trypsin in the form of static quenching, formed a stable complex at 1:1, and changed the conformation of trypsin. The results of thermodynamic constant showed that ΔG 
ISSN:0038-7010
1532-2289
DOI:10.1080/00387010.2019.1635162