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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: Aug 18, 2025

Millisecond Hydrogen/Deuterium-Exchange Mass Spectrometry for the Study of Alpha-Synuclein Structural Dynamics Under Physiological Conditions

Millisecond Hydrogen/Deuterium-Exchange Mass Spectrometry for the Study of Alpha-Synuclein Structural Dynamics Under Physiological Conditions

Published on: June 23, 2022

Modulation of α-synuclein phase separation by biomolecules.

Leandro Cruz Rodríguez¹, Nahuel N Foressi¹, M Soledad Celej¹

¹Departamento de Química Biológica Ranwel Caputto, Centro de Investigaciones en Química Biológica de Córdoba (CIQUIBIC, CONICET), Facultad de Ciencias Químicas, Universidad Nacional de Córdoba, Haya de la Torre y Medina Allende, Ciudad Universitaria, X5000HUA Córdoba, Argentina.

Biochimica Et Biophysica Acta. Proteins and Proteomics

|December 8, 2022

Summary

This summary is machine-generated.

Aberrant liquid-liquid phase separation (LLPS) links to neurodegenerative diseases. This study shows alpha-synuclein and Tau proteins can form mixed droplets, potentially driving Parkinson

Keywords:

Amyloids Heterotypic coacervates Intrinsically disordered protein Liquid-liquid phase separation Protein aggregation

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Area of Science:

Biochemistry
Neuroscience
Molecular Biology

Background:

Liquid-liquid phase separation (LLPS) is crucial for cellular functions.
Aberrant LLPS is implicated in neurodegenerative diseases like Parkinson's (PD) and Alzheimer's (AD).
Proteins forming pathological aggregates often undergo LLPS.

Purpose of the Study:

To investigate the phase separation behavior of alpha-synuclein (AS).
To examine AS interaction with ATP, polyamines, and Tau protein.
To explore the role of mixed protein condensates in PD and AD pathogenesis.

Main Methods:

Evaluated homotypic and heterotypic phase behavior of alpha-synuclein.
Studied interactions with ATP, polyamines, and Tau protein.
Characterized droplet formation and phase properties.

Main Results:

Alpha-synuclein (AS) shows low propensity for homotypic droplet formation.
AS phase separation is modulated by interacting biomolecules, forming liquid-like or solid-like phases.
Synergistic droplet formation observed between AS and Tau.

Conclusions:

Interactions with specific biomolecules influence AS phase separation.
Co-phase separation of AS and Tau supports their role in overlapping pathologies.
Mixed AS/Tau condensates may contribute to the biogenesis of neurodegenerative diseases.