Study on interaction between ginsenosides Rg_1,Rb_1 and Ro and bovine serum albumin.
10.19540/j.cnki.cjcmm.20190321.208
- Author:
Tian ZUO
1
;
Yue-Yang SUN
1
;
Wen-Lai XUE
1
;
Ying ZHANG
1
;
Guang WANG
1
;
Xiao-Hai ZHANG
1
;
Ran XU
1
;
Shao-Peng ZHANG
1
Author Information
1. College of Biological and Pharmaceutical Engineering,Wuhan Polytechnic University Wuhan 430070,China.
- Publication Type:Journal Article
- Keywords:
bovine serum albumin;
ginsenoside;
interaction;
molecular docking
- MeSH:
Animals;
Binding Sites;
Cattle;
Computer Simulation;
Ginsenosides;
chemistry;
Molecular Docking Simulation;
Protein Binding;
Serum Albumin, Bovine;
chemistry;
Spectrometry, Fluorescence;
Thermodynamics
- From:
China Journal of Chinese Materia Medica
2019;44(12):2559-2565
- CountryChina
- Language:Chinese
-
Abstract:
Small molecules with physiological or pharmacological activities need to interact with biological macromolecules in order to function in the body. As the protein with the highest proportion of plasma protein,serum albumin is the main protein binding to various endogenous or exogenous small molecules. Serum albumin interacts with small molecules in a reversible non-covalent manner and transports small molecules to target sites. Bovine serum albumin( BSA) is an ideal target protein for drug research because of its low cost and high homology with human serum albumin. The research on the interaction between drugs and BSA has become a hotspot in the fields of pharmacy,medicine,biology and chemistry. In this research,molecular docking method was used to study the interaction between three small ginsenosides with high pharmacological value( Rg_1,Rb_1,Ro) and bovine serum albumin( BSA),and the binding mode information of three ginsenosides interacting with BSA was obtained. The results of molecular docking showed that ginsenosides and amino acid residues in the active pocket of proteins could be combined by hydrophobic action,hydrogen bonding and electrostatic action. The interaction between small ginsenosides and bovine serum albumin is not the only form,and their interaction has many forms of force. The interaction between these molecules and various weak forces is the key factor for the stability of the complex. The results of this study can provide the structural information of computer simulation for the determination of the interaction patterns between active components and proteins of ginseng.
