The interaction between Tamoxifen (TMX) and Human serum Transferrin (hTf) was studied at physiological condition by using fluorescence, Synchronous fluorescence and circular dichroism spectroscopic. The resultes showed that a remarkable fluorescence decrease of hTf is called quenching. Quenching properties of drug-serum transferrin complex, differentiation between static and dynamic quenching. Changes in the environment of the aromatic residues and Maximum emission wavelength that indicated the structure of Trp and Tyr residues environments was altered and physiological functions of hTf were affected by TMX and the formation of TMX-hTf inclusion complexes. In addition, the alterations of protein secondary structure were qualitatively and quantitatively determined by the evidence from synchronous fluorescence and circular dichroism. This study is expected to provide important insight into the interactions of the physiological important protein with TMX in drug design.

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