Abstract：The interaction between osthole and human serum albumin(HSA) was investigated by fluorescence,UV-vis absorption,Fourier transform infrared(FT-IR) and circular dichroism(CD) spectroscopy under simulative physiological conditions.The results suggested that the intrinsic fluorescence of HSA was quenched by osthole was probably a result of the formation of osthole-HSA complex.The calculated thermodynamic parameters indicated that the binding of osthole to HSA was driven mainly by hydrophobic interaction.The site markers competitive experiments revealed that the binding of osthole to HSA mainly took place in site Ⅲ.The binding distance between osthole and HSA was determined to be 3.99nm based on the Frster theory.The results of FT-IR and CD spectra showed that the binding of osthole to HSA could induce partial changes in the second structure of the protein.
胡玉婷； 张国文. 蛇床子素与人血清白蛋白相互作用的光谱学特征[J]. 南昌大学学报（理科版）, 2012, 36(03): 250-.
HU Yu-ting,ZHANG Guo-wen. Spectroscopic studies of interaction between osthole and human serum albumin. , 2012, 36(03): 250-.
2012, Vol. 36 
