Interaction Between Lobetyolin and Bovine Serum Albumin by Steady-State Fluorescence and Molecular Docking
10.13422/j.cnki.syfjx.20201313
- VernacularTitle:稳态荧光技术及分子对接模拟研究党参炔苷与牛血清蛋白的相互作用
- Author:
Duan LI
1
;
Jun-yang YUAN
1
;
Jia HOU
1
;
Shi-jun SHAO
2
;
Fu-de YANG
1
Author Information
1. Gansu University of Chinese Medicine， Lanzhou 730000， China
2. Lanzhou Institute of Chemical Physics， Chinese Academy of Sciences， Lanzhou 730000， China
- Publication Type:Research Article
- Keywords:
lobetyolin;
bovine serum albumin;
steady-state fluorescence;
molecular-docking;
static quenching
- From:
Chinese Journal of Experimental Traditional Medical Formulae
2020;26(12):162-169
- CountryChina
- Language:Chinese
-
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.
