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Chin. Phys. B, 2021, Vol. 30(8): 088701    DOI: 10.1088/1674-1056/ac0690
INTERDISCIPLINARY PHYSICS AND RELATED AREAS OF SCIENCE AND TECHNOLOGY Prev   Next  

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
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.
Keywords:  amyloid      fast green      aggregation      Alzheimer's disease  
Received:  15 May 2021      Revised:  26 May 2021      Accepted manuscript online:  29 May 2021
PACS:  87.15.-v (Biomolecules: structure and physical properties)  
  87.14.E- (Proteins)  
  31.15.xv (Molecular dynamics and other numerical methods)  
  68.37.Ps (Atomic force microscopy (AFM))  
Fund: 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.
Corresponding Authors:  Wenhui Zhao, Dongdong Lin     E-mail:  zhaowenhui@nbu.edu.cn;lindongdong@nbu.edu.cn

Cite this article: 

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 2021 Chin. Phys. B 30 088701

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