AFM and STM study of β-amyloid aggregation on graphite

@inproceedings{Wang2003AFMAS,
  title={AFM and STM study of β-amyloid aggregation on graphite},
  author={Z Wang and Chunqing Zhou and Chen Wang and Li-Jun Wan and Xiaohong Fang and Chunli Bai},
  year={2003}
}
Abstract Atomic force microscopy (AFM) and scanning tunneling microscopy (STM) have been employed in situ and ex situ to directly study the aggregation of β -amyloid(1-42) (A β 42) peptide on hydrophobic graphite. From in situ AFM images, A β 42 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… CONTINUE READING

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Interprotofilament interactions between Alzheimer's Abeta1-42 peptides in amyloid fibrils revealed by cryoEM.

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