【作者】 马洪敏； 王晋； 刘树元； 闫涛； 于伟； 李燕； 魏琴；

【Author】 Hongmin Ma, Jin Wang, Shuyuan Liu, Tao Yan, Wei Yu, Yan Li and *Qin Wei School of Chemistry & Chemical Engineering, Jinan University, 250022, Jinan

【机构】 济南大学化学化工学院；

【Abstract】 The interaction between LG (Lumogallion) and BSA (bovine serum albumin) was studied by fluorescence quenching technique. Fluorescence data revealed that the fluorescence quenching of BSA caused by the addition of LG was a static quenching. Based on the F?rster’s theory of non-radiation energy transfer, the combination distance between BSA with LG was investigated to be 2.70 nm, which also indicated that the intrinsic fluorescence quenching of BSA caused by LG was a static one from other aspect. The thermodynamic parameters, ?H, ?G, ?S, calculated at different temperatures indicated that hydrogen bond and vander-waals forces played a major role in the interaction between LG and BSA.更多还原