Tunable inhibition of β-amyloid peptides by fast green molecules

doi:10.1088/1674-1056/ac0690

中国物理B ›› 2021, Vol. 30 ›› Issue (8): 88701-088701.doi: 10.1088/1674-1056/ac0690

Tunable inhibition of β-amyloid peptides by fast green molecules

Tiantian Yang(杨甜甜)¹, Tianxiang Yu(俞天翔)¹, Wenhui Zhao(赵文辉)^1,†, and Dongdong Lin(林冬冬)^1,2,‡

1 Department of Microelectronic Science and Engineering, Department of Physics, School of Physical Science and Technology, Ningbo University, Ningbo 315211, China;
2 Qian Xuesen Collaborative Research Center of Astrochemistry and Space Life Sciences, Ningbo University, Ningbo 315211, China

收稿日期:2021-05-15 修回日期:2021-05-26 接受日期:2021-05-29 出版日期:2021-07-16 发布日期:2021-07-23
通讯作者: Wenhui Zhao, Dongdong Lin E-mail:zhaowenhui@nbu.edu.cn;lindongdong@nbu.edu.cn
基金资助:
Project supported by the National Natural Science Foundation of China (Grand No. 11804174), Qian Xuesen Collaborative Research Center of Astrochemistry and Space Life Sciences, and K. C. Wong Magna Fund in Ningbo University.

Tunable inhibition of β-amyloid peptides by fast green molecules

Tiantian Yang(杨甜甜)¹, Tianxiang Yu(俞天翔)¹, Wenhui Zhao(赵文辉)^1,†, and Dongdong Lin(林冬冬)^1,2,‡

1 Department of Microelectronic Science and Engineering, Department of Physics, School of Physical Science and Technology, Ningbo University, Ningbo 315211, China;
2 Qian Xuesen Collaborative Research Center of Astrochemistry and Space Life Sciences, Ningbo University, Ningbo 315211, China

Received:2021-05-15 Revised:2021-05-26 Accepted:2021-05-29 Online:2021-07-16 Published:2021-07-23
Contact: Wenhui Zhao, Dongdong Lin E-mail:zhaowenhui@nbu.edu.cn;lindongdong@nbu.edu.cn
Supported by:
Project supported by the National Natural Science Foundation of China (Grand No. 11804174), Qian Xuesen Collaborative Research Center of Astrochemistry and Space Life Sciences, and K. C. Wong Magna Fund in Ningbo University.

摘要/Abstract

摘要： The aggregation of β-amyloid (Aβ) protein into toxic intermediates and mature fibrils is considered to be one of the main causes of Alzheimer's disease (AD). Small molecules as one of blockers are expected to be the potential drug treatment for the disease. However, the nucleation process in molecular assembly is less informative in the literatures. In this work, the formation of Aβ (16-22) peptides was investigated with the presence of small molecule of fast green (FG) at the initial aggregation stage. The results exhibited the tunable inhibitory ability of FG molecules on Aβ (16-22) peptides. Atomic force microscopy (AFM) demonstrated that the inhibitory effect would be dependent on the dose of FG molecules, which could delay the lag time (nucleation) and form single layer conjugates. Spectral measurements further showed that the β-sheet secondary structure of Aβ (16-22) reduced dramatically after the presence of FG molecules. Instead, non-β-sheet nanosheets were formed when the FG/Aβ (16-22) ratio reached 1:1. In addition, the cytotoxicity of aggregates reduced greatly with the presence of FG molecules compared with the Aβ (16-22) fibrils. Overall, this study provided a method for suppressing the toxic amyloid aggregates by FG molecules efficiently, and also showed a strategy for fabrication of two-dimensional materials by small molecules.

关键词: amyloid, fast green, aggregation, Alzheimer's disease

Abstract: The aggregation of β-amyloid (Aβ) protein into toxic intermediates and mature fibrils is considered to be one of the main causes of Alzheimer's disease (AD). Small molecules as one of blockers are expected to be the potential drug treatment for the disease. However, the nucleation process in molecular assembly is less informative in the literatures. In this work, the formation of Aβ (16-22) peptides was investigated with the presence of small molecule of fast green (FG) at the initial aggregation stage. The results exhibited the tunable inhibitory ability of FG molecules on Aβ (16-22) peptides. Atomic force microscopy (AFM) demonstrated that the inhibitory effect would be dependent on the dose of FG molecules, which could delay the lag time (nucleation) and form single layer conjugates. Spectral measurements further showed that the β-sheet secondary structure of Aβ (16-22) reduced dramatically after the presence of FG molecules. Instead, non-β-sheet nanosheets were formed when the FG/Aβ (16-22) ratio reached 1:1. In addition, the cytotoxicity of aggregates reduced greatly with the presence of FG molecules compared with the Aβ (16-22) fibrils. Overall, this study provided a method for suppressing the toxic amyloid aggregates by FG molecules efficiently, and also showed a strategy for fabrication of two-dimensional materials by small molecules.

Key words: amyloid, fast green, aggregation, Alzheimer's disease

中图分类号: (Biomolecules: structure and physical properties)

87.15.-v

87.14.E- (Proteins) 31.15.xv (Molecular dynamics and other numerical methods) 68.37.Ps (Atomic force microscopy (AFM))

Tiantian Yang(杨甜甜), Tianxiang Yu(俞天翔), Wenhui Zhao(赵文辉), and Dongdong Lin(林冬冬). Tunable inhibition of β-amyloid peptides by fast green molecules[J]. 中国物理B, 2021, 30(8): 88701-088701.

Tiantian Yang(杨甜甜), Tianxiang Yu(俞天翔), Wenhui Zhao(赵文辉), and Dongdong Lin(林冬冬). Tunable inhibition of β-amyloid peptides by fast green molecules[J]. Chin. Phys. B, 2021, 30(8): 88701-088701.

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Tunable inhibition of β-amyloid peptides by fast green molecules

Tunable inhibition of β-amyloid peptides by fast green molecules

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