Thermodynamic and functional changes of alpha-chymotrypsin after interaction with gallic acid.

Seyedeh Zohreh Vahedi, Sadegh Farhadian, Behzad Shareghi, Sanaz Asgharzadeh

Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy 2024 May 15

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In the present study, the interaction mechanism between gallic acid (GA) and α-Chymotrypsin (α-CT) was investigated by employing a series ofspectroscopic methods, computational docking and molecular dynamic (MD) simulation. Fluorescence spectra analysis indicated the formation of a stable complex between GA and α-CT, where the quenching of the fluorescence emission was predominantly characterized by a static mechanism. TheCA obtained binding constants for the α-CT-GA complex were in the order of 103 M-1, indicating the moderate binding affinity of GA for α-CT. The corresponding CD findings showed that the interaction between GA and α-CT resulted in an alteration of the protein's secondary structure. The findings of the enzyme activity investigation clearly showed that the presence of GA led to a notable decline in the enzymatic activity of α-CT, highlighting GA's function as an effective inhibitor for α-CT. The molecular docking simulations revealed the optimal binding site for the GA molecule within the α-CT structure and MD simulations confirmed the stability of the α-CT-GA complex. This research expands our comprehension regarding the behavior of enzymes in the presence of small-molecule ligands and opens avenues for food safety. Copyright © 2024 Elsevier B.V. All rights reserved.

Citation

Seyedeh Zohreh Vahedi, Sadegh Farhadian, Behzad Shareghi, Sanaz Asgharzadeh. Thermodynamic and functional changes of alpha-chymotrypsin after interaction with gallic acid. Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy. 2024 May 15;313:124109