文献类型：期刊文献

英文题名：Single molecule study of initial structural features on the amyloidosis process

作者：Hu, Yong-Xu[1,2];Ying, Yi-Lun[1,2];Gu, Zhen[1,2];Cao, Chan[1,2];Yan, Bing-Yong[3];Wang, Hui-Feng[3];Long, Yi-Tao[1,2]

机构：[1]E China Univ Sci & Technol, Key Lab Adv Mat, Shanghai 200237, Peoples R China;[2]E China Univ Sci & Technol, Dept Chem, Shanghai 200237, Peoples R China;[3]E China Univ Sci & Technol, Sch Informat Sci & Engn, Shanghai 200237, Peoples R China

年份：2016

卷号：52

期号：32

起止页码：5542

外文期刊名：CHEMICAL COMMUNICATIONS

收录：;WOS:【SCI-EXPANDED(收录号:WOS:000374035800009)】；

基金：This work was supported by the National Natural Science Foundation of China (21327807 and 21505043). Y.-L. Ying is supported by the 57th Chinese Post-doctor Fund (2015M570336).

语种：英文

摘要：We employed an alpha-hemolysin (alpha-HL) nanopore as a single-molecule tool to investigate the effects of initial structure on the amyloidosis process. The differences in the initial structure of two beta-amyloid (A beta) peptides (A beta 25-35 and A beta 35-25) could be distinguished in real-time due to their characteristic blockades. More importantly, the distinct aggregate dynamics for these two kinds of A beta fragments can be readily analyzed by monitoring the blockade frequency over time.