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Amyloid Fibrils

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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,...

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Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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Updated: Mar 18, 2026

A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis

A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis

Published on: May 22, 2018

Structural differences between amyloid beta oligomers.

Leonid Breydo¹, Dmitry Kurouski², Suhail Rasool³

¹Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697, United States; Department of Molecular Medicine and Byrd Alzheimer's Institute, University of South Florida, Tampa, FL 33612, United States.

Biochemical and Biophysical Research Communications

|July 2, 2016

Summary

This summary is machine-generated.

Soluble amyloid-beta (Aβ) oligomers in Alzheimer's disease exist in different structural forms. This study reveals fibrillar Aβ oligomers are less stable, while prefibrillar forms are partially disordered.

Keywords:

Alzheimer’s disease Amyloid beta Oligomers Protein aggregation

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Area of Science:

Neuroscience
Biochemistry
Structural Biology

Background:

Soluble amyloid-beta (Aβ) oligomers are implicated in Alzheimer's disease pathogenesis.
Aβ oligomer levels correlate with cognitive impairment.
Previous work categorized Aβ oligomers into structural classes using conformation-dependent antibodies.

Purpose of the Study:

To analyze the structures of Aβ40 oligomers within two distinct classes: fibrillar and prefibrillar.
To provide additional structural insights into these Aβ oligomer forms.

Main Methods:

Structural analysis of Aβ40 oligomers.
Categorization based on reactivity with conformation-dependent antibodies.
Assessment of oligomer stability towards denaturation.

Main Results:

Fibrillar Aβ40 oligomers exhibit structural similarity to fibrils but reduced stability.
Prefibrillar Aβ40 oligomers display a partially disordered structure.
Findings align with and expand upon previously proposed structural models.

Conclusions:

Distinct structural characteristics of fibrillar and prefibrillar Aβ40 oligomers are elucidated.
Structural differences may influence their roles in Alzheimer's disease.
Further understanding of Aβ oligomer structures is crucial for therapeutic development.