Binding to proteins will effectively decrease the concentration of free drugs, benefit their metabolic modification .Interaction between the tamoxifen, HB was investigated by fluorescence spectroscopy. HB is the most abundant blood protein and tamoxifen interact with this macromolecule that crucially determines their bioavailability. In the spectral range of 300-400nm tamoxifen and their phenyl subsitued derivatives show two main fluorescence bands commonly r+ by suppressed vibrational fine structure. In the spectral range of 300-500nm HB show one main fluorescence peak referred to as peak (340nm). The fluorescence intensity of tamoxifen enhanced regularly with the increasing HB concentration ,the shift of the emission maximum tamoxifen to 340 nm is observed. The intrinsic fluorescence of HB-- 37 Trp that plays a key role in the quaternary state change upon ligand binding---37 Trp is 340nm. Changes in emission spectra tamoxifen are common in response to drug conformational transitions, substrate binding and interaction between tamoxifen and HB .As a result of specific binding of tamoxifem to HB.

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