Investigating the interaction mechanisms between arachin and resveratrol: Utilizing multi-spectroscopy and computational chemistry.

Xue Peng, Qi Gao, Ning Wang, Miao Yu, Yu-Qi Yang, Shi-Qi Yue, Jing-Li Xin, Jia-Jia Rao, You-Lin Xue

Journal: Food chemistry 2024;463(Pt 4):141435

PMID: 39378718

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Abstract

Arachin (ARA) and resveratrol (RES) are the primary protein and bioactive compound in peanuts and their processed products. However, the mechanism of interaction between these two substances remained unclear. To investigate protein structural changes, conformational variations, and molecular mechanisms in the interaction between them, multispectral analysis and computational chemistry methods were employed. Experimental results confirmed that RES quenched ARA's intrinsic fluorescence through static quenching, indicating their interaction. Thermodynamic analysis revealed the interaction between them was endothermic, spontaneous, and primarily hydrophobic. Molecular dynamics (MD) simulations highlighted strong affinity between RES and ARA, with key amino acids (His425, Val426, Phe405, and Phe464) facilitating their interaction. RES binding increased stability without significant protein conformational changes. The independent gradient model based on Hirshfeld partition (IGMH) validated their interaction, emphasizing van der Waals (VDW) interactions and hydrogen bonds (H-bonds) as crucial for stable binding. This research lays a theoretical foundation for potential applications of ARA-RES complex products in the food industry.

Address: College of Light Industry, Liaoning University, Shenyang 110036, China.; College of Light Industry, Liaoning University, Shenyang 110036, China; Department of Regional Economic Development, Party School of Liaoning Provincial Party Committee, Shenyang 110161, China.; College of Materials Science and Technology, Beijing Forestry University, Beijing 100083, China.; Institute of Food and Processing, Liaoning, Academy of Agricultural Sciences, Shenyang 110161, China.; Department of Plant Sciences, North Dakota State University, Fargo, ND 58108, USA.; College of Light Industry, Liaoning University, Shenyang 110036, China. Electronic address: [email protected].

DOI: 10.1016/j.foodchem.2024.141435

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MeSH Terms: Resveratrol, Thermodynamics, Molecular Dynamics Simulation, Arachis, Hydrogen Bonding, Hydrophobic and Hydrophilic Interactions, Stilbenes, Protein Binding, Spectrometry, Fluorescence, Computational Chemistry