The binding of wogonin with bovine serum albumin (BSA) was investigated at different temperatures by fluorescence, circular dichroism (CD) and Fourier transform infrared spectroscopy (FT-IR) at pH7.40. The association constants K were determined by Stern-Volmer equation based on the quenching of the fluorescence of BSA in the presence of wogonin, which were in agreement with the constants calculated by Scatchard plots. The thermodynamic parameters were calculated according to the Van't Hoff equation and the result indicated that DeltaH(0) and DeltaS(0) had a negative value (-12.02 kJ/mol) and a positive value (58.72 J/mol K), respectively. On the basis of the displacement experimental and the thermodynamic results, it is considered that wogonin binds to site I (subdomain IIA) of BSA mainly by hydrophobic interaction. The studied results by FT-IR and CD experiment indicated that the secondary structures of protein have been perturbed by the interaction of wogonin with BSA.