Abstract: Under simulated physiological conditions, the interaction between solanesol and bovine serum albumin(BSA) was investigated. The quenching constant, binding constant, the number of binding site and binding distance were determined by fluorescence spectroscopy and ultraviolet absorption spectroscopy. They were 1.76×10⁷ and 2.7×10⁷ mol/L, 1.54×10⁶ and 1.9×10⁶ mol/L, 1.09 and 1.50, and r=0 nm at 25 ℃ and 37 ℃, respectively. Thermodynamic parameters were ΔG<0,ΔH>0,ΔS>0. So the fluorescence of bovine serum albumin was strongly quenched by solanesol in the static quenching style. Thermodynamics analysis demonstrated that the hydrophobic interaction force played a main role in the binding of solanesol with bovine serum albumin and solanesol was inserted into bovine serum albumin at tryptophan 212.

Key words: fluorescence spectroscopy, UV spectroscopy, solanesol, bovine serum albumin, fluorescence quenching