The investigation of the interaction between NCP-EDA and bovine serum albumin by spectroscopic approaches

► The interaction between BSA and NCP-EDA was investigated by spectroscopic methods. ► The fluorescence quenching mechanism is dynamic and static quenching. ► Hydrophobic interaction force plays a major role in stabilizing the complex. ► The binding constants, ΔG, ΔH, and ΔS of the interaction were calculated. ► The conformation of BSA is changed in the presence of NCP-EDA.