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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: Dec 18, 2025

Exogenous Administration of Microsomes-associated Alpha-synuclein Aggregates to Primary Neurons As a Powerful Cell Model of Fibrils Formation

Exogenous Administration of Microsomes-associated Alpha-synuclein Aggregates to Primary Neurons As a Powerful Cell Model of Fibrils Formation

Published on: June 26, 2018

α-Synuclein aggregation nucleates through liquid-liquid phase separation.

Soumik Ray¹, Nitu Singh¹, Rakesh Kumar¹

¹Department of Biosciences and Bioengineering, IIT Bombay, Mumbai, India.

Nature Chemistry

|June 10, 2020

Summary

This summary is machine-generated.

Liquid-liquid phase separation of alpha-synuclein (α-Syn) precedes its aggregation in Parkinson's disease pathogenesis. This process, involving droplet formation and maturation, is promoted by disease-associated factors.

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Area of Science:

Neuroscience
Biochemistry
Molecular Biology

Background:

Alpha-synuclein (α-Syn) aggregation is a key hallmark of Parkinson's disease (PD).
The initial steps driving α-Syn aggregation and amyloid formation remain incompletely understood.
Understanding early events is crucial for developing effective PD therapeutics.

Purpose of the Study:

To investigate the early events in α-Syn aggregation.
To determine if liquid-liquid phase separation (LLPS) precedes α-Syn aggregation.
To elucidate the role of LLPS in Parkinson's disease pathogenesis.

Main Methods:

In vitro reconstitution of α-Syn.
Cellular models of α-Syn aggregation.
Microscopy and biochemical assays to analyze α-Syn phase separation and aggregation.

Main Results:

Liquid-like droplets of α-Syn form in vitro and mature into amyloid hydrogels.
Factors exacerbating PD, including low pH and mutations, promote α-Syn LLPS.
Cellular α-Syn droplets form and mature into perinuclear aggresomes, regulated by microtubules.

Conclusions:

Liquid-liquid phase separation is an early, critical step in α-Syn aggregation.
LLPS of α-Syn is modulated by factors relevant to Parkinson's disease.
This study provides mechanistic insights into α-Syn pathogenesis and potential therapeutic targets.