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Amyloid Fibrils

Amyloid 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 Fibrils

Amyloid 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...

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Related Experiment Video

Updated: May 22, 2026

Selection of Aptamers for Amyloid β-Protein, the Causative Agent of Alzheimer's Disease

Selection of Aptamers for Amyloid β-Protein, the Causative Agent of Alzheimer's Disease

Published on: May 14, 2010

Towards a pharmacophore for amyloid.

Meytal Landau¹, Michael R Sawaya, Kym F Faull

¹Howard Hughes Medical Institute, UCLA-DOE Institute for Genomics and Proteomics, Department of Biological Chemistry, University of California, Los Angeles, California, United States of America.

|June 23, 2011

Summary

Researchers visualized atomic structures of Alzheimer's disease proteins and small molecule binders. These findings offer a molecular framework for developing new diagnostics and treatments for protein aggregation diseases.

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Area of Science:

Biochemistry
Structural Biology
Neuroscience

Background:

Alzheimer's disease and related disorders are challenging to diagnose and treat.
Amyloid fibers are implicated in the pathology of these neurodegenerative diseases.
Understanding the molecular interactions within amyloid fibers is crucial for therapeutic development.

Purpose of the Study:

To determine the atomic structures of fiber-forming protein segments involved in Alzheimer's disease.
To investigate the binding interactions of small molecules with these protein segments.
To provide a molecular basis for designing diagnostics and therapeutics for protein aggregation diseases.

Main Methods:

X-ray microcrystallography was employed to determine high-resolution atomic structures.
Fiber-like complexes of protein segments and small molecule binders were analyzed.
Structural analysis focused on the arrangement of beta-sheets and small molecule binding sites.

Main Results:

Atomic structures revealed fiber-like complexes composed of paired beta-sheets.
Small molecules were observed to bind within the inter-sheet space, parallel to the fiber axis.
Apolar molecules showed nonspecific binding, while the negatively charged Orange-G specifically bound to lysine residues.

Conclusions:

The determined structures provide a molecular framework for understanding amyloid fiber formation.
Insights into small molecule binding interactions can guide the design of targeted therapies.
This research facilitates the development of novel diagnostics and drugs for Alzheimer's and other protein aggregation diseases.