苦荞蛋白（2S/13S）与膳食酚类的比较研究：对蛋白质结构、结合位点及功能的影响

Comparative study of dietary phenols with Tartary buckwheat protein (2S/13S): impact on structure, binding sites and functionality of protein.

作者信息

Li Dongze, Zhu Ling, Wu Qiming, Chen Yiling, Wu Gangcheng, Zhang Hui

机构信息

School of Food Science and Technology, Jiangnan University, Wuxi, China.

National Engineering Research Center for Functional Food, Jiangnan University, Collaborative Innovation Center of Food Safety and Quality Control in Jiangsu Province, Wuxi, China.

出版信息

J Sci Food Agric. 2024 Jan 30;104(2):698-706. doi: 10.1002/jsfa.12960. Epub 2023 Oct 26.

DOI:10.1002/jsfa.12960

PMID:37653274

Abstract

BACKGROUND

This research was to investigate the interaction mechanism between 2S albumin and 13S globulin (2S and 13S, the most important storage proteins in Tartary buckwheat seeds) and three phenols (rutin, quercetin and myricetin) regarding the structural and antioxidant properties of their complexes.

RESULTS

There are differences in the binding affinity of phenols for 2S and 13S. Rutin had a higher binding affinity for 2S, myricetin had a higher binding affinity for 13S, and 13S exhibited a higher affinity toward phenols than did 2S. Binding with phenols significantly changed the secondary and tertiary structures of 2S and 13S, decreased the surface hydrophobic value and enhanced the antioxidant capacity. Molecular docking and isothermal titration calorimetry showed that the binding processes were spontaneous and that there were hydrogen bonds, hydrophobic bonds and van der Waals force interactions between phenols and proteins.

CONCLUSION

摘要

背景

本研究旨在探究苦荞种子中最重要的贮藏蛋白2S白蛋白和13S球蛋白（2S和13S）与三种酚类物质（芦丁、槲皮素和杨梅素）之间的相互作用机制，以及它们复合物的结构和抗氧化特性。

结果

酚类物质对2S和13S的结合亲和力存在差异。芦丁对2S的结合亲和力较高，杨梅素对13S的结合亲和力较高，且13S对酚类物质的亲和力高于2S。与酚类物质结合显著改变了2S和13S的二级和三级结构，降低了表面疏水性值并增强了抗氧化能力。分子对接和等温滴定量热法表明，结合过程是自发的，酚类物质与蛋白质之间存在氢键、疏水键和范德华力相互作用。