Multiple spectroscopic studies on the interaction between olaquindox, a feed additive, and bovine serum albumin

The interaction between olaquindox (OLA) and bovine serum albumin (BSA) was investigated using fluorescence, UV-vis absorption and circular dichroism (CD) spectroscopy. The results showed that the fluorescence quenching of BSA by OLA was a static quenching process induced by the formation of OLA-BSA complex. The binding constant of OLA-BSA complex was calculated to be 1.299 × 104 L mol−1 (293 K). The negative values of ΔH0 and ΔS0 indicated that hydrogen bond and van der Waals interactions played major roles in stabilizing the complex. Site probe competition experiments and number of binding sites (n) revealed that OLA could bind to site I in subdomain IIA of BSA, and the binding distance (r) was evaluated to be 3.643 nm according to Förster's non-radiative energy transfer theory. The results of CD and three-dimensional fluorescence spectra suggested some conformational changes of BSA after OLA binding.

► The fluorescence quenching of bovine serum albumin (BSA) by olaquindox was static. ► Hydrogen bond and van der Waals interactions were the main binding forces. ► The binding and energy transfer of olaquindox to BSA occurred in subdomain IIA. ► BSA's conformation was changed after olaquindox binding.