Zinc binding strength of proteins dominants zinc uptake in Caco-2 cells,RSC Advances

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Zinc binding strength of proteins dominants zinc uptake in Caco-2 cells
RSC Advances ( IF 3.9 ) Pub Date : 2022-08-01 , DOI: 10.1039/d2ra03565k
Tian Li ₁ , Ruonan Jiao ₁ , Jiaqi Ma ₁ , Jiachen Zang ₁ , Guanghua Zhao ₁ , Tuo Zhang ₁

Affiliation

Zinc plays a vital role in structural, catalysis, and signal regulation in the human body. Zinc deficiency leads to the dysfunction of many organs and immunity systems. Diet proteins have distinct effects on zinc uptake. However, the mechanisms are uncovered. Here we select three principal components from whey protein: alpha-lactalbumin, beta-lactoglobulin, and bovine serum albumin, which bind with zinc at different affinities, to evaluate the relationship between their potential zinc uptake and protein binding. The experimental data shows that beta-lactoglobulin could promote zinc uptake, alpha-lactalbumin has minor effects, whereas bovine serum albumin reduced zinc uptake in Caco-2 cell lines. Zinc binding effects on protein structure were thoroughly inspected through fluorescent spectroscopy and X-ray crystallography. Isothermal titration calorimetry revealed that three proteins have different binding affinities toward zinc ions. We speculate that protein binding eliminates toxic effects from free zinc, and the binding strength dominates zinc uptake.

中文翻译：

蛋白质的锌结合强度在 Caco-2 细胞中占主导地位

锌在人体的结构、催化和信号调节中起着至关重要的作用。锌缺乏会导致许多器官和免疫系统的功能障碍。饮食蛋白质对锌的吸收有明显的影响。然而，这些机制未被发现。在这里，我们从乳清蛋白中选择三个主要成分：α-乳清蛋白、β-乳球蛋白和牛血清白蛋白，它们与锌以不同的亲和力结合，以评估它们潜在的锌吸收与蛋白质结合之间的关系。实验数据表明，β-乳球蛋白可以促进锌的吸收，α-乳白蛋白的作用较小，而牛血清白蛋白会降低 Caco-2 细胞系的锌吸收。通过荧光光谱和 X 射线晶体学彻底检查了锌对蛋白质结构的结合作用。等温滴定量热法显示三种蛋白质对锌离子具有不同的结合亲和力。我们推测蛋白质结合消除了游离锌的毒性作用，并且结合强度支配了锌的吸收。

更新日期：2022-08-01

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