The investigation of the interaction between edaravone and bovine serum albumin by spectroscopic approaches

► We explored the interaction of BSA and EDA using spectroscopic methods. ► The fluorescence quenching mechanism is combined quenching. ► Hydrophobic interaction force plays a major role in stabilizing the complex. ► The binding constants, binding sites, and thermodynamic parameters were calculated. ► EDA affects the conformation of tryptophan residue's microregion.