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

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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.

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

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Publication details

The article was received on 17 Apr 2019, accepted on 06 Aug 2019 and first published on 07 Aug 2019


Article type: Paper
DOI: 10.1039/C9MT00088G
Metallomics, 2019, Advance Article

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

    D. Cheng, X. Wang, J. Tang, X. Zhang, C. Wang and H. Li, Metallomics, 2019, Advance Article , DOI: 10.1039/C9MT00088G

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