the investigation of the interaction between human serum transferring with colchicine in the presence of pb+2 ions: synchronous fluorescence measurements

the interaction between holo-transferin (htf) and colchicine (col) was investigated in the present of pb +2 ions under physiological conditions by using synchronous fluorescence spectra. the synchronous fluorescence spectra show a slight change of tryptophan residue micro-environment. synchronous fluorescence spectra show that the structure of the tyrosine residue environment was altered by interaction of the col and pb +2 ions with htf. the fluorescence intensity of htf decreased regularly beside a small blue shift with increasing concentrations of col and pb +2 ions. the intrinsic fluorescence of htf was quenched in the presence of drug and ion. interaction of drugs with htf and htf-pb +2 can elucidate the properties of drug-protein and ion- protein complex, as it may provide useful information about the structural feature that determines the therapeutic effectiveness of ion and drugs. therefore, it has become a significant research field in life science, chemistry, biotechnology and clinical medicine.