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| Activation of Epigallocatechin Gallate on Alcohol Dehydrogenase:
Multispectroscopy and Molecular Docking Methods |
| ZHANG Xiao-dan1, 2, LIU Li-li1*, YU Ying1, CHENG Wei-wei1, XU Bao-cheng1, HE Jia-liang1, CHEN Shu-xing1, 2 |
1. College of Food and Bioengineering, Henan University of Science and Technology, National Experimental Teaching Demonstration Center for Food Processing and Security, Henan International Joint Laboratory of Food Processing and Quality and Safety Control, Research and Utilization of Functional Food Resources Science and Technology Innovation Team of Henan Provincial Department of Education, Luoyang 471023, China
2. Food Laboratory of Zhongyuan, Luohe 462300, China
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Abstract Alcohol dehydrogenase (ADH) plays a key role in the pathway of alcohol metabolism. By activating ADH activity, the absorption of alcohol can be promoted to relieve alcoholism and protect the liver. This paper studied the interaction between ADH and epigallocatechin gallate (EGCG). The binding mechanism of ADH and EGCG was investigated by UV-Vis spectrum, fluorescence spectrum, Fourier infrared spectrum and molecular docking method. The thermal denaturation temperatures of ADH and EGCG-ADH complex were measured by differential scanning calorimeter, and then the thermal stability changes of the complex EGCG were analyzed. EGCG was characterized by scanning electron microscope. The results showed that EGCG activated the catalytic activity of ADH, and the activation rate was 33.33%. The effect of EGCG on ADH caused its microenvironment and secondary structure changes, forming a complex with anumber of binding sites close to 1, and van der waals force and hydrogen bond played an important role in its stability. Compared with ADH, the α-helix content in the secondary structure of the complex decreased, and the β-sheet content increased. In addition, the molecular docking results further confirmed that the hydrogen bond between the hydroxyl group of the EGCG benzene ring and the surrounding amino acids is beneficial to maintain the stability of the complex. In addition, the van der waals force and n-alkyl between EGCG and ADH are the main reasons for the activation of ADH activity. The above results proved that EGCG can activate the catalytic activity of ADH by combining with ADH, which can provide theoretical guidance for the preparation of safer and more efficient alternatives to hangovers.
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Received: 2022-09-07
Accepted: 2023-06-26
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Corresponding Authors:
LIU Li-li
E-mail: yangliuyilang@126.com
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