Affinity capillary electrophoresis was employed to study the interaction between tabersonine(TAB) and bovine serum albumin (BSA). The results showed that the binding constant is 8.00×106L·mol-1under normal temperature. The thermodynamic parameters indicated that the interaction between tabersonine and BSA was driven mainly by hydrophobic interaction and van der Waals forces. The secondary structure of BSA was changed in the presence of TAB according to the FT-IR results. It was shown that TAB reduced α-helix, β-turn and increased β-sheet. At the molecular level, the binding mode of TAB and BSA was determined by molecular modeling method.
