期刊
ULTRAMICROSCOPY
卷 97, 期 1-4, 页码 73-79出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/S0304-3991(03)00031-7
关键词
atomic force microscopy; scanning tunneling microscopy; beta-amyloid; Alzheimer disease
类别
Atomic force microscopy (AFM) and scanning tunneling microscopy (STM) have been employed in situ and ex situ to directly study the aggregation of beta-amyloid(1-42) (Abeta42) peptide on hydrophobic graphite. From in situ AFM images, Abeta42 peptides were seen to aggregate into the sheets that preferred to three orientations with characteristic 3-fold symmetry (Proc. Natl. Acad. Sci. USA 96 (1999) 3688). The sheets were formed by parallel narrow lines with a height of 0.8-1.0 nm and a width of 12-14 run. The narrow lines looked like beaded chains and have a right-handed axial periodicity. The high-resolufion ex situ AFM and STM images showed that sonic fibrils of beta-amyloid had a characteristic domain texture, indicating they were formed through the association of protofibrils and monomers. The fibril containing lateral associated filaments that exhibited right-handed twist was clearly observed in the STM image. These results provide important clues to study the detailed structure of beta-amyloid aggregates and the mechanism of the Abeta fibrils formation on hydrophobic surface. (C) 2003 Elsevier Science B.V. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据