A study on the binding interaction between the imidazole derivative and bovine serum albumin by fluorescence spectroscopy

► Interactions between dfppip and BSA were investigated by fluorescence quenching. ► Quenching mechanism mainly arise from the formation of BSA-imidazole complex. ► D→A distance is <8 nm indicates that the energy transfer from BSA to dfppip. ► Synchronous fluorescence spectra to exploit the structural change of BSA. ► Effect of other ions on the binding constants between dfppip and BSA.