Interaction Between Lobetyolin and Bovine Serum Albumin by Steady-State Fluorescence and Molecular Docking / 中国实验方剂学杂志

ABSTRACT

Objective:The interaction between lobetyolin and bovine serumal bumin（bovine serum albumin，BSA）. Method:By the steady-state fluorescence analysis method，the molecular-docking，ultraviolet absorption spectrum and fluorescence quenching were used to calculate quenching constant and binding constant，the number of sites，the position，the force and the distance of lobetyolin-BSA system. In addition， the effect of metalionson quenching constant of the lobetyolin-BSA system was studied. Result:The quenching constant was 1.25×104 L·mol-1（37 ℃），the binding constant was 2.95×104 L·mol-1（37 ℃），and the number of sites was 1 and bound with site 1 in ⅡA of BSA， thermodynamic meters were ΔH=-19.374 kJ·mol-1，ΔS=23.1 J·mol-1·K-1， the interaction distance was 3.2 nm. Meta lions could accelerate the quenching. Conclusion:By the steady-state fluorescence technique，molecular-docking and ultraviolet absorption spectrum，the quenching mechanism of Lobetyolin-BSA is quiescent quenching，and the interactive force is electro static force. The Lobetyolin-BSA can be well combined. At the same time，it also shows that the molecular docking results are similar to the experimental results obtained by steady-state fluorescence analysis.