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Spectroscopic and computational studies on the binding interaction between gallic acid and Pin1
Guo Fei Zhu1, Shao Li Lyu2, Yang Liu3
1Institute of Food and Drug Manufacturing Engineering, Guizhou Institute of Technology, Guiyang, China.
Luminescence : the Journal of Biological and Chemical Luminescence
|September 7, 2021
Summary
Gallic acid (GA) directly binds to peptidyl-prolyl cis/trans isomerase Pin1, inhibiting its activity. This interaction, driven by weak forces, suggests potential therapeutic applications for Pin1-related diseases.
Area of Science:
- Biochemistry
- Molecular Biology
- Pharmacology
Background:
- Gallic acid (GA) is a natural compound with health benefits and anti-tumor properties.
- Peptidyl-prolyl cis/trans isomerase (Pin1) is crucial in preventing malignant tumor development.
Purpose of the Study:
- To investigate the interaction between Gallic acid (GA) and Pin1.
- To determine if GA affects Pin1 activity and its structural properties.
Main Methods:
- Systematic investigation using multiple spectral methods.
- Computational analysis to understand binding interactions.
- Enzyme activity assays to assess functional impact.
Main Results:
- Gallic acid binds directly to Pin1 with moderate affinity (10^4 mol/L).
- The binding is mediated by van der Waals forces, hydrogen bonds, and electrostatic interactions.
- GA binding reduces Pin1 activity by altering its conformational characteristics, involving key residues Lys63, Arg68, and Arg69.
Conclusions:
- Gallic acid interacts with and inhibits Pin1 activity.
- This inhibition affects Pin1's structural and functional properties.
- The findings suggest GA as a potential therapeutic agent for Pin1-related diseases.
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