Abstract
The aim of this present work is to investigate the interaction between doxorubicin and bovine serum albumin (BSA) in simulated physiological conditions by spectroscopic methods to reveal potential toxic effects of the drug. The results reflected that doxorubicin made the fluorescence quenching of BSA through a static quenching procedure. The binding constants at 293, 298, and 303 K were obtained as 2.53 × 105, 8.13 × 104, and 3.59 × 104 M–1, respectively. There may be one binding site of doxorubicin on BSA. The thermodynamic parameters indicated that the interaction between doxorubicin and BSA was driven mainly by hydrogen bonding and electrostatic forces. Synchronous fluorescence spectra and circular dichroism (CD) results showed doxorubicin binding slightly changed the conformation of BSA with secondary structural content changes. Forster resonance energy transfer (FRET) study revealed high possibility of energy transfer with doxorubicin-Trp-212 distance of 3.48 nm. The results of the present study may provide valuable information for studying the distribution, toxicological and pharmacological mechanisms of doxorubicin in vivo.
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