Investigation of the Aggregation Process of Amyloid-β-(16-22) Peptides and the Dissolution of Intermediate Aggregates

被引：30

作者：

Lin, Dongdong ^{[1
]}

Luo, Yin ^{[1
]}

Wu, Shan ^{[1
]}

Ma, Qianqian ^{[1
]}

Wei, Guanghong ^{[1
]}

Yang, Xinju ^{[1
]}

机构：

[1] Fudan Univ, State Key Lab Surface Phys, Shanghai 200433, Peoples R China

来源：

LANGMUIR | 2014年 / 30卷 / 11期

基金：

中国国家自然科学基金; 上海市自然科学基金;

关键词：

AMYLOID-FIBRIL FORMATION; THIOFLAVIN-T-BINDING; BETA-SHEET; ALZHEIMERS-DISEASE; CONFORMATIONAL-ANALYSIS; A-BETA(16-22) PEPTIDE; PROTEIN AGGREGATION; MECHANISM; OLIGOMERS; INHIBITION;

D O I：

10.1021/la4048165

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

The aggregation processes of amyloid-beta-(16-22) peptides (A beta(16-22)) are investigated by atomic force microscopy (AFM). It is found that A beta(16-22) peptides quickly aggregate from monomers to oligomers and flakelike structures and finally to fibrils. In particular, unusual morphology change is observed in an early stage of aggregation; that is, the originally formed flakelike structures would disappear in the following aggregation processes. To determine the evolution of the flakelike structures, in situ AFM imaging is carried out in liquid to reveal the real-time morphology change of A beta(16-22). The results provide clear evidence that the flakelike structures are in an unstable intermediate state, which would be dissolved into oligomers or short protofibrils for reorganization. Further fluorescence and attenuated total reflectance Fourier transform infrared (ATR-FTIR) experiments on thioflavin T(ThT) suggest that those flakelike structures contain beta-sheet components.

引用

页码：3170 / 3175

页数：6

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