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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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Updated: Aug 27, 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

Free Gangliosides Can Alter Amyloid-β Aggregation.

Arghya Chakravorty¹, Samuel D McCalpin², Bikash R Sahoo^2,3

¹Department of Chemistry, University of Michigan, Ann Arbor, Michigan 48109, United States.

The Journal of Physical Chemistry Letters

|September 29, 2022

Summary

This summary is machine-generated.

Free ganglioside GM1 inhibits amyloid-β40 aggregation but not amyloid-β42. This suggests GM1

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Published on: March 7, 2019

Area of Science:

Neuroscience
Biochemistry
Computational Biology

Background:

Alzheimer's disease is characterized by amyloid-β (Aβ) peptide aggregates.
The lipid-chaperone hypothesis proposes that free lipids influence Aβ aggregation.
Neuronal ganglioside GM1 is abundant in mammalian brains.

Purpose of the Study:

To investigate the effects of ganglioside GM1 on the aggregation of Aβ40 and Aβ42 isoforms.
To explore the molecular interactions between GM1 and Aβ peptides using simulations and experiments.

Main Methods:

All-atom molecular dynamics simulations in explicit solvent.
Nuclear magnetic resonance (NMR) experiments.
Thioflavin T fluorescence assays to assess aggregation.

Main Results:

Free GM1 forms stable, water-soluble complexes with both Aβ40 and Aβ42.
NMR confirms well-ordered, compact GM1+Aβ complexes.
Aβ40 prefers GM1-containing hetero-oligomers; Aβ42 prefers GM1-lacking homo-oligomers.
GM1 inhibits Aβ40 aggregation dose-dependently but not Aβ42 aggregation.

Conclusions:

GM1's differential effects on Aβ40 and Aβ42 aggregation are explained by isoform-specific binding preferences.
This study provides molecular insights into how lipids modulate amyloidogenic peptide aggregation.
Findings support the lipid-chaperone hypothesis in the context of Alzheimer's disease pathogenesis.