Studies on the interaction between troxerutin and bovine serum albumin / 中国药理学通报

ABSTRACT

Aim To study the characteristics of the binding reaction of Troxetutin with bovine serum albumin (BSA) by fluorescence and ultra violet-visible absorption spectra.Methods The quenching mechanism of the fluorescence of BSA by troxerutin was studied with fluorescence.To determine the dynamic quenching constants and static binding constants,the Stern-Volmer equation and the double reciprocal Lineweaver-Burk equation were applied. The number of binding site was calculated with double logarithmic equation and the main binding force was discussed by thermodynamic equations. The binding distance and energy transfer efficiency between donor (BSA) and acceptor (troxerutin) were obtained effectively quenched fluorescence of BSA via static quenching processes. The binding constant Ka was calculated to be in the order of 106,indicating a strong interaction between Troxerutin and BSA. The number of binding site was approximately equal to 1,the binding distance was 1.97 nm,the energy transfer efficiency was 0.529,and the binding force was mainly hydrophobic force.Conclusion Troxerutin effectively quenchs the intrinsic fluorescence of BSA via static quenching mechanism,and the binding is mainly driven by the hydrophobic interaction.