Molecular basis of cross-interactions between Aβ and Tau protofibrils probed by molecular simulations

Fufeng Liu; Luying Jiang; Jingcheng Sang; Fuping Lu; Li Li

Your Location：

Home >

Browse articles >

Molecular basis of cross-interactions between Aβ and Tau protofibrils probed by molecular simulations

Full Length Article | Updated：2026-01-06

- Molecular basis of cross-interactions between Aβ and Tau protofibrils probed by molecular simulations
- Chinese Journal of Chemical Engineering Vol. 55, Issue 3, Pages: 173-180(2023)
- Affiliations：
  
  1. State Key Laboratory of Food Nutrition and Safety, Key Laboratory of Industrial Fermentation Microbiology of Ministry of Education, Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, Tianjin University of Science & Technology,Tianjin,China,300457
  2. College of Marine and Environmental Science, Tianjin University of Science & Technology,Tianjin,China,300457
- Author bio：
- Funds：
- DOI：
  CLC：
- Published：2023
- Accepted：
Scan QR Code
Fufeng Liu, Luying Jiang, Jingcheng Sang, Fuping Lu, Li Li. Molecular basis of cross-interactions between Aβ and Tau protofibrils probed by molecular simulations[J]. Chinese Journal of Chemical Engineering, 2023, 55(3): 173-180.
DOI：

Fufeng Liu, Luying Jiang, Jingcheng Sang, Fuping Lu, Li Li. Molecular basis of cross-interactions between Aβ and Tau protofibrils probed by molecular simulations[J]. Chinese Journal of Chemical Engineering, 2023, 55(3): 173-180. DOI：

摘要

Abstract

Amyloid β-protein (Aβ) and Tau

two common pathogenic proteins associated with Alzheimer’s disease (AD)

cross-interact

and thus co-assemble into hybrid aggregates. However

molecular mechanism of the cross-interactions remains unclear. To explore the issue

docking and molecular dynamics (MD) simulations were coupled to study the cross-interactions between Aβ pentamer and Tau pentamer. Four stable hybrid decamer conformations including double layer

single layer

block

and part-in were obtained by protein-protein docking software HADDOCK 2.2. Then

MD simulations were used to explore the molecular mechanism of cross-interactions between Aβ pentamer and Tau pentamer. The results of MD simulations showed that the part-in structure was the most stable among all the above four representative ones. The binding energy between Aβ and Tau was about -759.77 kJ·mol

-1

in the part-in structure. Moreover

the part-in conformation would undergo conformational transition

which would improve its hydrophobicity and make the structure more compact. This work offers a structural understanding of cross-interactions between Aβ and Tau linked to AD.

关键词

Keywords

references

Views

Downloads

CSCD

Alert me when the article has been cited

Submit

Tools

Publicity Resources

Mechanistic insights into water desalination through two-dimensional MXene-graphene oxide membranes: A molecular simulation study

Green and low-viscosity deep eutectic solvents for the extraction of quinoline from wash oil: Experimental investigation and molecular dynamics simulation

The effect of ethylene-vinyl acetate copolymer on the formation process of wax crystals and hydrates

Rational surface charge engineering of haloalkane dehalogenase for boosting the enzymatic performance in organic solvent solutions

Molecular dynamics simulations of ovalbumin adsorption at squalene/water interface

Related Author

Faquan Yu

Yanan Xue

Zijuan Li

Yibo Xu

Xiaoyan Tan

Jie Liu

Mengsha Han

Fan Yang

Related Institution

Hubei Key Laboratory for Novel Reactor and Green Chemistry Technology, WIT-Qianjiang Research Institute of Green Chemical Industry, School of Chemical Engineering and Pharmacy, Wuhan Institute of Technology

College of Chemistry and Chemical Engineering, Taiyuan University of Technology

State Key Laboratory of Heavy Oil Processing, China University of Petroleum-Beijing at Karamay

State Key Laboratory of Heavy Oil Processing, China University of Petroleum

Department of Biochemical Engineering, School of Chemical Engineering and Technology and Key Laboratory of Systems Bioengineering and Frontiers Science Center for Synthetic Biology (Ministry of Education), Tianjin University

⁰