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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: Jun 28, 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

14-3-3τ as a Modulator of Early α-Synuclein Multimerization and Amyloid Formation.

Gobert Heesink¹, Maxime C M van den Oetelaar², Slav A Semerdzhiev¹

¹Nanobiophysics, Faculty of Science and Technology, MESA + Institute for Nanotechnology and Technical Medical Centre, University of Twente, Enschede 7500 AE, The Netherlands.

ACS Chemical Neuroscience

|April 18, 2024

Summary

The protein 14-3-3τ delays alpha-synuclein aggregation, a key factor in Parkinson's disease. It forms mixed multimers, preventing toxic amyloid formation and offering new therapeutic targets for Parkinson's disease.

Keywords:

14-3-3 chaperone IDP multimerization modulation of multimerization protein co-condensation protein-protein interactions α-synuclein aggregation

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

Published on: June 26, 2018

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Last Updated: Jun 28, 2025

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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

Area of Science:

Neuroscience
Biochemistry
Molecular Biology

Background:

Alpha-synuclein (αS) aggregation is central to Parkinson's disease (PD) pathogenesis.
Cellular quality control mechanisms typically manage αS aggregation throughout life.
The protein 14-3-3τ is known to delay αS aggregation and PD onset, but its mechanism is unclear.

Purpose of the Study:

To elucidate the molecular mechanisms by which 14-3-3τ delays αS aggregation.
To investigate the early stages of αS multimerization and the role of 14-3-3τ.

Main Methods:

Microscale thermophoresis (MST) to study protein interactions.
Single-molecule burst analysis to quantify early αS multimers.
Data modeling to analyze multimerization dynamics.

Main Results:

14-3-3τ delays αS aggregation in a concentration-dependent manner.
Early αS multimers are nanoscale condensates forming cooperatively, preceding fibril nucleation.
14-3-3τ shifts the mechanism to form smaller, non-cooperative mixed multimers (αS/14-3-3τ) that do not form amyloid.

Conclusions:

14-3-3τ intervenes in early αS multimerization, preventing aggregation and maintaining αS solubility and function.
This mechanism provides novel targets for pharmacological intervention in Parkinson's disease.