AI Article Synopsis
- Arachin (ARA) is a protein and resveratrol (RES) is a bioactive compound found in peanuts, and their interaction was studied to understand how they affect each other on a molecular level.
- Using multispectral analysis and computational chemistry, researchers found that RES can quench ARA's intrinsic fluorescence and that their interaction is endothermic, spontaneous, and driven mainly by hydrophobic forces.
- Molecular dynamics simulations revealed that specific amino acids play a key role in the strong affinity between ARA and RES, and the study's findings support potential food industry applications for their complex.
Article 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.
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| http://dx.doi.org/10.1016/j.foodchem.2024.141435 | DOI Listing |
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