Molecular dynamic investigate the affection of EGFR by Tubemoside

Tubemoside as a common traditional Chinese medicine is playing an important role in the field of prevention and treatment of lung cancer without any side effects. However, the reason and its mechanism remain unclear. In our study, the molecular dynamic simulation was used to investigate the mechanis...

Full description

Saved in:
Bibliographic Details
Published in:Journal of molecular graphics & modelling 2019-05, Vol.88, p.203-208
Main Authors: Du, Xia, Chen, Zhi-yong, Guo, Dong, Zhang, Hong, Liu, Yang, Wang, Chun-liu, Sun, Ting-ting, Shi, Long-fei, Li, Ye, Liu, Feng
Format: Article
Language:English
Subjects:
Drugs, Chinese Herbal - chemistry
Electrostatic interaction
Epidermal growth factor receptor (EGFR)
ErbB Receptors - chemistry
ErbB Receptors - genetics
Humans
Hydrogen bond network analysis
Hydrogen Bonding
Molecular dynamic (MD) simulation
Molecular Dynamics Simulation
Principal component analysis
Protein Binding
Protein Conformation
Saponins - chemistry
Static Electricity
Structure-Activity Relationship
Tubemoside
Citations: Items that this one cites
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Tubemoside as a common traditional Chinese medicine is playing an important role in the field of prevention and treatment of lung cancer without any side effects. However, the reason and its mechanism remain unclear. In our study, the molecular dynamic simulation was used to investigate the mechanism at the molecular level. We found that the hydrogen bond network of proteins (three states of EGFR) was affected by Tubemoside. The movement and opening/closing state of protein was changed when combine with Tubemoside. The results of principal component analysis were used to prove the transform of proteins and the change of its movement. Electrostatic interactions of proteins also were studied. The numbers of active interaction sites will decrease while Tubemoside emerged in the protein, which will cause the activity change of EGFR for forming asymmetric dimers required for activation. [Display omitted] •The molecular dynamic simulation was used to investigate the mechanism.•The opening/closing state of proteins was changed according to the hydrogen bond.•The PCA were used to prove the transform of proteins and the change of its movement.•The active interaction sites will decrease while Tubemoside emerged in the protein.
ISSN:1093-3263
1873-4243
DOI:10.1016/j.jmgm.2019.01.017