Insights into the cross-amyloid aggregation of Aβ40 and its N-terminal truncated peptide Aβ11-40 affected by epigallocatechin gallate

doi:10.1016/j.cjche.2021.04.018

中国化学工程学报 ›› 2022, Vol. 45 ›› Issue (5): 284-293.DOI: 10.1016/j.cjche.2021.04.018

Insights into the cross-amyloid aggregation of Aβ₄₀ and its N-terminal truncated peptide Aβ_11-40 affected by epigallocatechin gallate

Yue Liang, Wenjuan Wang, Yan Sun, Xiaoyan Dong

Department of Biochemical Engineering and Key Laboratory of Systems Bioengineering (Ministry of Education), School of Chemical Engineering and Technology, Tianjin University, Tianjin 300354, China

收稿日期:2020-12-22 修回日期:2021-03-29 出版日期:2022-05-28 发布日期:2022-06-22
通讯作者: Xiaoyan Dong,E-mail:d_xy@tju.edu.cn
基金资助:
The work was funded by the National Natural Science Foundation of China (21978207 and 21621004) and the Natural Science Foundation of Tianjin from Tianjin Municipal Science and Technology Commission (19JCZDJC36800).

Insights into the cross-amyloid aggregation of Aβ₄₀ and its N-terminal truncated peptide Aβ_11-40 affected by epigallocatechin gallate

Yue Liang, Wenjuan Wang, Yan Sun, Xiaoyan Dong

Department of Biochemical Engineering and Key Laboratory of Systems Bioengineering (Ministry of Education), School of Chemical Engineering and Technology, Tianjin University, Tianjin 300354, China

Received:2020-12-22 Revised:2021-03-29 Online:2022-05-28 Published:2022-06-22
Contact: Xiaoyan Dong,E-mail:d_xy@tju.edu.cn
Supported by:
The work was funded by the National Natural Science Foundation of China (21978207 and 21621004) and the Natural Science Foundation of Tianjin from Tianjin Municipal Science and Technology Commission (19JCZDJC36800).

摘要/Abstract

摘要： Inhibition of protein misfolding and aggregation is a great challenge in the field of biochemical and biopharmaceutical engineering. Alzheimer's disease (AD) is a protein-misfolding disease, and the interactions between 40-amino-acid-residue β-amyloid peptide (Aβ₄₀) and its N-terminal truncated peptide Aβ_11-40 demonstrate that Aβ_11-40 may play an important role in the pathological process of AD. However, the effect of inhibitors on Aβ_11-40 aggregation and on the cross-amyloid aggregation (co-assembly) between Aβ₄₀ and Aβ_11-40 has never been studied. Herein, coaggregation and seeding interactions between Aβ₄₀ and Aβ_11-40 as well as the effect of epigallocatechin gallate (EGCG), a small molecule inhibitor, on the cross-amyloid aggregation have been investigated by extensive analyses. It is found that Aβ_11-40 participates in the aggregation of Aβ₄₀ and leads to the formation of coaggregates that contain less β-sheet structures than pure Aβ₄₀ aggregates. The aggregation kinetics along with morphologies and secondary structures of the coaggregates are also significantly affected by the Aβ₄₀/Aβ_11-40 ratio. EGCG accelerates the nucleation of Aβ₄₀ but retards that of Aβ_11-40 by affecting their elongation and secondary nucleation processes in solution and on solid surfaces. Meanwhile, EGCG makes the conformations of the seeding-induced Aβ aggregates more compact, especially for the homologous seedings. Isothermal titration calorimetry measurement indicates that hydrophobic interactions mainly contribute to the inhibition of the two Aβ isoforms by EGCG. The findings of this research have provided new insights into Aβ aggregation and the effect of an important inhibitor and the results would benefit in the development of potent inhibitors against co-assembly of different amyloid proteins.

关键词: Protein, Aggregation, Kinetics, Nucleation, Elongation, Molecular interactions

Abstract: Inhibition of protein misfolding and aggregation is a great challenge in the field of biochemical and biopharmaceutical engineering. Alzheimer's disease (AD) is a protein-misfolding disease, and the interactions between 40-amino-acid-residue β-amyloid peptide (Aβ₄₀) and its N-terminal truncated peptide Aβ_11-40 demonstrate that Aβ_11-40 may play an important role in the pathological process of AD. However, the effect of inhibitors on Aβ_11-40 aggregation and on the cross-amyloid aggregation (co-assembly) between Aβ₄₀ and Aβ_11-40 has never been studied. Herein, coaggregation and seeding interactions between Aβ₄₀ and Aβ_11-40 as well as the effect of epigallocatechin gallate (EGCG), a small molecule inhibitor, on the cross-amyloid aggregation have been investigated by extensive analyses. It is found that Aβ_11-40 participates in the aggregation of Aβ₄₀ and leads to the formation of coaggregates that contain less β-sheet structures than pure Aβ₄₀ aggregates. The aggregation kinetics along with morphologies and secondary structures of the coaggregates are also significantly affected by the Aβ₄₀/Aβ_11-40 ratio. EGCG accelerates the nucleation of Aβ₄₀ but retards that of Aβ_11-40 by affecting their elongation and secondary nucleation processes in solution and on solid surfaces. Meanwhile, EGCG makes the conformations of the seeding-induced Aβ aggregates more compact, especially for the homologous seedings. Isothermal titration calorimetry measurement indicates that hydrophobic interactions mainly contribute to the inhibition of the two Aβ isoforms by EGCG. The findings of this research have provided new insights into Aβ aggregation and the effect of an important inhibitor and the results would benefit in the development of potent inhibitors against co-assembly of different amyloid proteins.

Key words: Protein, Aggregation, Kinetics, Nucleation, Elongation, Molecular interactions

Yue Liang, Wenjuan Wang, Yan Sun, Xiaoyan Dong. Insights into the cross-amyloid aggregation of Aβ₄₀ and its N-terminal truncated peptide Aβ_11-40 affected by epigallocatechin gallate[J]. 中国化学工程学报, 2022, 45(5): 284-293.

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Insights into the cross-amyloid aggregation of Aβ₄₀ and its N-terminal truncated peptide Aβ_11-40 affected by epigallocatechin gallate

Insights into the cross-amyloid aggregation of Aβ₄₀ and its N-terminal truncated peptide Aβ_11-40 affected by epigallocatechin gallate

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