Abstract

The interaction of bisphenol A with bovine hemoglobin (BHb) under physiological conditions was investigated by using fluorescence, ultraviolet–visible (UV-Vis) absorption, circular dichroism (CD), and molecular modeling. The experimental results showed that BPA can bind with BHb to form a complex. The binding constant Ka and the number of binding sites <i>n</i> were calculated to be 1.49 × 10<sup>5</sup> L mol<sup>–1</sup> and 1, respectively. Molecular modeling study revealed that BPA bound into BHb central cavity, and the binding mode of BPA–BHb complex could be hydrogen bonding. The UV-Vis absorption and CD spectra indicated that the secondary structure of BHb was altered, which may affect physiological functions of hemoglobin. This work is helpful for clarifying the molecular toxic mechanism of BPA in vivo.

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