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

doi:10.1016/j.cjche.2022.04.021

中国化学工程学报 ›› 2023, Vol. 55 ›› Issue (3): 173-180.DOI: 10.1016/j.cjche.2022.04.021

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

Fufeng Liu¹, Luying Jiang¹, Jingcheng Sang¹, Fuping Lu¹, Li Li²

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 300457, China;
2. College of Marine and Environmental Science, Tianjin University of Science & Technology, Tianjin 300457, China

收稿日期:2022-02-07 修回日期:2022-04-18 出版日期:2023-03-28 发布日期:2023-06-03
通讯作者: Fufeng Liu,E-mail:fufengliu@tust.edu.cn;Li Li,E-mail:lili_2016@tust.edu.cn
基金资助:
This work was funded by the National Natural Science Foundation of China (21908165 and 21878234) and Regional Innovation System Project (21ZYQCSY00050).

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

Fufeng Liu¹, Luying Jiang¹, Jingcheng Sang¹, Fuping Lu¹, Li Li²

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 300457, China;
2. College of Marine and Environmental Science, Tianjin University of Science & Technology, Tianjin 300457, China

Received:2022-02-07 Revised:2022-04-18 Online:2023-03-28 Published:2023-06-03
Contact: Fufeng Liu,E-mail:fufengliu@tust.edu.cn;Li Li,E-mail:lili_2016@tust.edu.cn
Supported by:
This work was funded by the National Natural Science Foundation of China (21908165 and 21878234) and Regional Innovation System Project (21ZYQCSY00050).

摘要/Abstract

摘要： 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: Alzheimer's disease, Amyloid β-protein, Tau, Cross-interactions, Protein-protein docking, Molecular dynamics simulation

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.

Key words: Alzheimer's disease, Amyloid β-protein, Tau, Cross-interactions, Protein-protein docking, Molecular dynamics simulation

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]. 中国化学工程学报, 2023, 55(3): 173-180.

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.

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

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