Study On The Interaction Between Effective Components Of Chinese Herbs And Bovine Serum Albumins By Fluorescence

Fluorescence method has been applying to study in biochemistry, medicine, industry and chemistry. There are many virtues such as high sensitivity, high selectivity, simple spectrum and prompt analysis, so the use of it is increasing steadilyFluorescence quenching is a physical process or chemical process in witch the fluorescent intensity decreases, when something reacts with fluorescent molecule. Using the process of fluorescence quenching, we can set up an analytic method, fluorescence quenching method. Fluorescence quenching method usually has higher sensitivity and higher selectivity then others. Furthermore, we can use this method to study diffusing speed of quenchers. In biochemistry, we can also use this method to study the location of the combine and form of albuminoid.Albuminoid has endogenous fluorescence. It can be a donor to react with an acceptor. Because forming coordination compound, the albuminoid endogenous fluorescence quenches. Blood serum is the most abundant carrier albumen in blood plusma. It has important academic and practical significance to study the interaction between medicines and serum albumins.In this series papers, three effective components of Chinese herbs have been studied. The binding reactions between Quercetin ( QCT ) and bovine serum albumins ( BSA ), Puerarin( PR ) and bovine serum albumins( BSA ), Rutin( RT ) and bovine serum albumins( BSA) in aqueous solution have been studied separately by fluorescence and UV-VIS absorption spectra. The results indicate that the combination reactions of them are static quenching processes. In aqueous solution, QCT, PR, RT bound strongly with BSA at 25°C and 37°C, respectively. The binding constants (K₍B(QCT)=1.12×10⁶ L·mol^-1,K₍B(RT)=6.64×10⁴ L·mol^-1,K_{B(PR)=1.37×10⁶ L·mol^-1}, the shortest binding distance ( r _QCT=3.69 nm,r_RT=4.82 nm,r_PR=3.44 nm ) and the energy transfer efficiencies (E_QCT=0.317,E _RT=0.0359,E_PR=0.670) between BSA donor and acceptors ( QCT, RT, PR ) have been obtained by Forster's nonradiative energy transfer mechanism. According to the thermodynamic parameters, the main types of binding force between them have been suggested.