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

Abstract

The widespread use of aluminum in drinking water, food, agriculture and pharmaceuticals has greatly increased the risk of human exposure to excess aluminum, which is a serious hazard to human health. In our previous work, serum albumin was observed to have a specific affinity for aluminum. However, the mechanism of binding of aluminum to serum albumin is 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 spontaneous endothermic reaction. The binding force is mainly hydrophobic 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 is enhanced after the combination of Al-Mal. This study can provide a theory evidence for the binding mechanism of food-borne aluminum and serum albumin. Keywords: aluminum-maltol; bovine serum albumin; ligand binding; spectroscopy; molecular docking

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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, Accepted Manuscript

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    Characterization of the binding 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, Accepted Manuscript , DOI: 10.1039/C9MT00088G

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