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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,...

Amyloid Fibrils

Amyloid Fibrils

Protein Folding

Protein Folding

Protein Folding

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...

Protein and Protein Structure

Protein and Protein Structure

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.
A protein's shape is critical to its function. For example, an enzyme...

Protein Organization

Protein Organization

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Related Experiment Video

Updated: Feb 26, 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

Amyloid beta: structure, biology and structure-based therapeutic development.

Guo-Fang Chen¹, Ting-Hai Xu¹, Yan Yan¹

¹VARI-SIMM Center, Center for Structure and Function of Drug Targets, CAS-Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.

Acta Pharmacologica Sinica

|July 18, 2017

Summary

Alzheimer's disease involves amyloid beta peptide (Aβ) accumulation, but its exact role and effective treatments remain elusive. This review explores Aβ structure, function, neurotoxicity, and emerging therapeutic strategies for Alzheimer's disease.

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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 13, 2010

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

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A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation

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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 13, 2010

Area of Science:

Neuroscience
Biochemistry
Pathology

Background:

Alzheimer's disease (AD) pathogenesis involves amyloid beta peptide (Aβ) accumulation.
The precise physiological and pathological roles of Aβ and its mechanism of dementia causation are not fully understood.
Current treatments for AD lack efficiency in halting or reversing disease progression.

Purpose of the Study:

To review the structure, biological functions, and neurotoxicity of Aβ.
To discuss Aβ receptors involved in its uptake, clearance, and metabolism.
To summarize therapeutic developments and novel strategies for Alzheimer's disease treatment.

Main Methods:

Literature review of Aβ structure, function, and neurotoxicity.
Analysis of potential Aβ receptors and their roles.
Summary of current and emerging therapeutic strategies for AD.

Main Results:

Aβ is implicated in AD pathogenesis, but its exact role and mechanisms of neurotoxicity require further elucidation.
Several potential receptors mediate Aβ interactions, influencing its brain dynamics.
A wide range of therapeutic strategies are under investigation, targeting Aβ, its receptors, and tau protein.

Conclusions:

Understanding Aβ's multifaceted roles is crucial for developing effective AD therapies.
Targeting Aβ, its receptors, or tau protein shows promise.
Novel agents and strategies, including small molecules, vaccines, and secretase modulators, offer potential for future AD treatment.