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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,...

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Related Experiment Video

Updated: Sep 22, 2025

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

Modulation of beta-amyloid aggregation using ascorbic acid.

Isabella Sampaio¹, Felipe Domingues Quatroni¹, Paula Maria Pincela Lins¹

¹GNano - Nanomedicine and Nanotoxicology Group, Physics Institute of São Carlos, University of São Paulo, CP 369, 13560-970, São Carlos, SP, Brazil.

|May 19, 2022

Summary

This summary is machine-generated.

Ascorbic acid (AA) inhibits Alzheimer's disease (AD) associated amyloid-β 1-42 (Aβ42) aggregation by binding to Aβ42 peptides. This interaction prevents Aβ42 strand stacking, offering potential therapeutic strategies for AD and other amyloid diseases.

Keywords:

Alzheimer's disease Amyloid inhibitor Ascorbic acid Beta-amyloid aggregation

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Preparation of Oligomeric β-amyloid1-42 and Induction of Synaptic Plasticity Impairment on Hippocampal Slices

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Preparation of Oligomeric β-amyloid1-42 and Induction of Synaptic Plasticity Impairment on Hippocampal Slices

Preparation of Oligomeric β-amyloid1-42 and Induction of Synaptic Plasticity Impairment on Hippocampal Slices

Published on: July 14, 2010

Area of Science:

Biochemistry
Neuroscience
Molecular Biology

Background:

Reduced ascorbic acid (AA) levels are observed in Alzheimer's disease (AD) brains.
The impact of AA on amyloid-β 1-42 (Aβ42) aggregation remains unclear.

Purpose of the Study:

To investigate the effect of ascorbic acid on Aβ42 aggregation.
To elucidate the molecular mechanisms underlying AA's interaction with Aβ42.

Main Methods:

Fluorescence assay
Circular dichroism
Atomic force microscopy
Isothermal titration calorimetry
Ligand docking
Molecular dynamics simulations

Main Results:

Ascorbic acid reduces Aβ42 fibril formation.
AA binds to Aβ42 peptides with high affinity.
AA binding site between β-strands inhibits Aβ42 oligomer stacking.

Conclusions:

Ascorbic acid exhibits a significant inhibitory effect on Aβ42 aggregation.
Understanding AA's molecular interactions with Aβ42 can guide novel therapeutic drug design for AD and other amyloidogenic diseases.