Abstract
ABSTRACTPolybrominated diphenyl ethers are vital flame retardants in production and human life and they are widespread global organic pollutants in the environment and likewise in food and feed, causing a potential health concern. Hemoglobin is the main protein in the blood, which is a carrier of oxygen in red blood cells. This work aimed at investigating the toxic interactions of polybrominated diphenyl ethers with hemoglobin, by molecular modeling and spectroscopic analysis methods. Decabrominated diphenyl ether and bovine hemoglobin were selected as representatives for polybrominated diphenyl ethers and hemoglobin, respectively. The experimental results indicated that decabrominated diphenyl ether changed the frames’ conformation and the microenvironment of bovine hemoglobin, which can affect the physiological function of the protein. Decabrominated diphenyl ether combined with bovine hemoglobin with the average number of binding sites (0.7) to form bovine hemoglobin–decabrominated diphenyl ether complex. The binding constant was 860.95 L mol−1. In addition, the molecular docking data revealed that the van der Waals forces played the primary role in the interaction between bovine hemoglobin and decabrominated diphenyl ether. The study provides insight into the molecular toxicity mechanism of decabrominated diphenyl ether during the blood transportation in vivo.
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