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牛血清白蛋白与麦芽酚相互作用时的结合机制和构象变化的表征:光谱和分子对接研究。

Characterization of the binding mechanism and conformational changes of bovine serum albumin upon interaction with aluminum-maltol: a spectroscopic and molecular docking study.

机构信息

State Key Laboratory of Food Nutrition and Safety, Tianjin University of Science & Technology, Tianjin, No. 29, 13th Avenue, Tianjin Economy Technological Development Area, 300457, Tianjin, China.

出版信息

Metallomics. 2019 Oct 16;11(10):1625-1634. doi: 10.1039/c9mt00088g.

DOI:10.1039/c9mt00088g
PMID:31453625
Abstract

The widespread use of aluminum in the treatment of drinking water, food, agriculture and pharmaceuticals has greatly increased the risk of human exposure to excess aluminum, which is a serious health hazard to human beings. In our previous work, serum albumin was reported to have a specific affinity for aluminum. However, the mechanism of binding of aluminum to serum albumin was unclear. In this work, the interaction between bovine serum albumin (BSA) and aluminum-maltol (Al-Mal) was studied by molecular docking and spectroscopic analysis. The results show that the combination of Al-Mal and BSA is a spontaneous endothermic reaction. The binding force is mainly related to the hydrophobic force and hydrogen bonding; when the ratio of BSA to Al-Mal was 1 : 10, the random coils of BSA increased by 47.6%. In addition, the hydrophobicity of BSA was enhanced after combining with Al-Mal. This study can provide a theoretical evidence for the binding mechanism of food-borne aluminum and serum albumin.

摘要

铝在饮用水、食品、农业和制药中的广泛应用大大增加了人类暴露于过量铝的风险,这对人类健康构成了严重威胁。在我们之前的工作中,已经报道了血清白蛋白对铝具有特异性亲和力。然而,铝与血清白蛋白结合的机制尚不清楚。在这项工作中,通过分子对接和光谱分析研究了牛血清白蛋白(BSA)与铝-麦芽酚(Al-Mal)之间的相互作用。结果表明,Al-Mal 与 BSA 的结合是一个自发的吸热反应。结合力主要与疏水作用力和氢键有关;当 BSA 与 Al-Mal 的比例为 1:10 时,BSA 的无规卷曲增加了 47.6%。此外,BSA 与 Al-Mal 结合后疏水性增强。这项研究可以为食物来源的铝与血清白蛋白的结合机制提供理论依据。

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