Interaction of Neferine with Bovine Serum Albumin
The interaction between neferine(NF)and bovine serum albumin(BSA)was studied under a pH 7.40 Tris-HCl buffer system by multiple spectroscopic techniques.It is shown that NF has a powerful ability to quench the albumin's fluorescence in a static mode.The fluorescence quenching data were analyzed according to Stern-Volmer equation and Line weaver-Burk equation.The binding constant obtained was 1.70×104 L/mol at 293 K and ΔH°=-20.2 kJ/mol,ΔS°=12.0 J/(K·mol).The main sorts of binding force of NF-BSA were hydrophobic interaction and electrostatic action.The distance between donor and acceptor in BSA-NF was 2.59 nm based on the Frster energy transfer theory.Results of technique of circular dichroism etc show the binding can cause conformation change of BSA.In the mean time,effects of bioactive components from traditional Chinese medicine(glycyrrhetinic acid)and fatty acids on the binding were evaluated.