Binding of β-casein with fluvastatin and pitavastatin

Abstract

In this work, the binding interaction of fluvastatin (FLU) and pit-avastatin (PIT) with bovine β-casein (β-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-β-CN and PIT-β-CN complexes, the intrinsic fluorescence of β-CN was quenched. The number of bound FLU and PIT per protein molecule (n) were about 1, also the binding constant of FLU-β-CN and PIT-β-CN complexes were 7.96×104 and 3.44×104 M-1 at 298 K, respectively. This result suggests that the binding affinity of FLU to β-CN was higher than that for PIT. Molecular modelling showed different binding sites for FLU and PIT on β-CN. All these experimental results suggest that β-CN can be used as a carrier protein which delivers FLU and PIT based drugs to target molecules.

Keywords

• milk protein
• statin
• molecular modeling
• spectroscopy