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Updated: Aug 14, 2026
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Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy
Published on: November 30, 2018
AFM and STM study of beta-amyloid aggregation on graphite
Zhigang Wang1, Chunqing Zhou, Chen Wang
1The Center for Molecular Sciences, Institute of Chemistry, Chinese Academy of Sciences, Beijing 100080, PR China.
Ultramicroscopy
|June 13, 2003
Summary
Atomic force microscopy and scanning tunneling microscopy revealed how beta-amyloid(1-42) (Abeta42) peptides aggregate into specific sheet structures on graphite. These findings offer insights into the formation mechanism of Abeta fibrils.
Area of Science:
- Biophysics
- Materials Science
- Nanotechnology
Background:
- Beta-amyloid (Abeta) peptide aggregation is central to neurodegenerative diseases.
- Understanding Abeta fibril formation is crucial for developing therapeutic strategies.
Purpose of the Study:
- To directly investigate the in situ and ex situ aggregation of beta-amyloid(1-42) (Abeta42) peptide on hydrophobic graphite surfaces.
- To elucidate the structural characteristics and formation mechanisms of Abeta aggregates.
Main Methods:
- In situ and ex situ Atomic Force Microscopy (AFM).
- In situ and ex situ Scanning Tunneling Microscopy (STM).
Main Results:
- Abeta42 peptides formed sheet-like aggregates with preferred orientations and 3-fold symmetry.
- Aggregates consisted of parallel narrow lines (0.8-1.0nm height, 12-14nm width) resembling beaded chains with right-handed axial periodicity.
- High-resolution AFM and STM revealed domain texture in fibrils, suggesting formation from protofibrils and monomers.
- STM images clearly showed fibrils with associated filaments exhibiting a right-handed twist.
Conclusions:
- The study provides direct structural insights into Abeta42 aggregation on hydrophobic surfaces.
- Findings contribute to understanding the detailed structure of beta-amyloid aggregates.
- The results offer clues regarding the mechanism of Abeta fibril formation.
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Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
03:03Amyloid Fibrils
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...