Synthesis and application of thiol-functionalized magnetic nanoparticles for studying interactions of epirubicin hydrochloride with bovine serum albumin by fluorescence spectrometry.

A novel method was developed for studying the interaction between epirubicin hydrochloride (EPI) and bovine serum albumin (BSA) by fluorescence spectrometry. Fe₃O₄ magnetic nanoparticles (MNPs) synthesized and functionalized with thiol group were employed for the immobilization and separation of target BSA in reaction solutions. The concentrations of the non-immobilized BSA and unbound EPI were obtained separately by fluorescence spectrometry. The binding constants ( K _a) and number of binding sites ( n) of EPI with BSA were calculated. In this study, the K _a value was 5.05 × 10⁵ L mol⁻¹, suggesting a strong binding of EPI to BSA, and the n value was 1.15. The effects of common metal ions on K _a of EPI with BSA were also investigated, and the results showed there was clearly bindings between the metal ions and BSA. The precise binding sites of EPI on BSA were determined as being in site I from the competitive displacement experiments. Copyright © 2016 John Wiley & Sons, Ltd. [ABSTRACT FROM AUTHOR]