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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: Apr 16, 2026

Labeling and Imaging of Amyloid Plaques in Brain Tissue Using the Natural Polyphenol Curcumin

Labeling and Imaging of Amyloid Plaques in Brain Tissue Using the Natural Polyphenol Curcumin

Published on: November 1, 2019

Curcumin Binding to Beta Amyloid: A Computational Study.

Praveen P N Rao¹, Tarek Mohamed^1,2, Karan Teckwani^1,2

¹School of Pharmacy, Health Sciences Campus, University of Waterloo, 200 University Avenue West, Waterloo, ON, N2L3G1, Canada.

Chemical Biology & Drug Design

|March 18, 2015

Summary

This summary is machine-generated.

Curcumin, found in turmeric, binds to amyloid aggregates, potentially preventing Alzheimer's disease. Molecular modeling shows curcumin stabilizes non-toxic amyloid structures, offering a new therapeutic avenue.

Keywords:

Alzheimer's disease amyloid fibril binding energy curcumin hexapeptide keto-enol molecular docking molecular dynamics

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Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy

Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy

Published on: November 30, 2018

Area of Science:

Biochemistry
Neuroscience
Computational Chemistry

Background:

Alzheimer's disease (AD) is linked to amyloid-beta (Aβ) peptide aggregation.
Curcumin, a turmeric compound, shows potential in preventing Aβ aggregation.
Systematic studies on curcumin's binding to Aβ oligomers and fibrils are lacking.

Purpose of the Study:

To investigate curcumin's binding affinity and stability with Aβ aggregates using computational models.
To understand curcumin's interaction mechanism with Aβ hexapeptide and full-length fibril assemblies.

Main Methods:

Construction of computational models for Aβ hexapeptide (16) KLVFFA(21) octamer and full-length Aβ fibril β-sheet assemblies.
Molecular docking and molecular dynamics (MD) simulations to evaluate curcumin binding.
Analysis of binding energy (Ebinding) and root-mean-square deviation (RMSD) for stability assessment.

Main Results:

Curcumin adopted a linear extended conformation parallel to the fiber axis in both models.
Curcumin exhibited greater binding stability in the Aβ hexapeptide octamer model (Ebinding = -10.05 kcal/mol) than in the full-length Aβ fibril model (Ebinding = -3.47 kcal/mol).
MD simulations indicated stable curcumin binding to the full-length Aβ fibril, causing fluctuations in the fibril spine region (HQKLVFFA).

Conclusions:

Curcumin binding to Aβ aggregates shifts the aggregation equilibrium.
Curcumin promotes the formation of non-toxic amyloid aggregates.
These findings support curcumin's therapeutic potential for Alzheimer's disease by modulating Aβ aggregation pathways.