Abstract: The binding characteristics and stability of coreopsin with CYP3A4/CYP2D6 was studied by  using spectroscopy analysis and computer simulation techniques. The results show that the intrinsic fluorescence of cytochrome P450 proteins (CYPs) is quenched mainly by static quenching and supplemented by dynamic quenching. The binding capacity of coreopsin with CYP3A4 is greater than that of CYP2D6. The coreopsin interacts with  CYPs to form a complex. The binding of coreopsin to CYPs leads to changes in  the secondary structure of CYPs. The coreopsin mainly binds to CYPs through hydrogen bonds and van der Waals forces. The  complex formed by coreopsin and two types of CYPs is stable.

Key words: coreopsin,  , cytochrome P3A4,  , cytochrome P2D6, binding characteristics,  ,  , stability