In this work, the binding interaction of fluvastatin (FLU) and pitavastatin (PIT) with bovine ?-casein (?-CN) were performed under physiological conditions (pH 7.2) by fluorescence emission spectroscopy, synchronous fluorescence spectroscopy, Fourier transform infrared spectroscopy (FTIR) and molecular docking methods. Due to the formation of FLU-?-CN and PIT-?-CN complexes, the intrinsic fluorescence of ?-CN was quenched. The number of bound FLU and PIT per protein molecule (n) were about 1, also the binding constant of FLU-?-CN and PIT-?-CN complexes were 7.96?104 and 3.44?104M-1 at 298 K, respectively. This result suggests that the binding affinity of FLU to ?-CN was higher than that for PIT. Molecular modeling showed different binding sites for FLU and PIT on ?-CN. All these experimental results suggest that ?.