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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, normally used to...

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, normally used to...

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Related Experiment Video

Updated: Jun 8, 2026

Generation of Alpha-Synuclein Preformed Fibrils from Monomers and Use In Vivo

Generation of Alpha-Synuclein Preformed Fibrils from Monomers and Use In Vivo

Published on: June 2, 2019

Human beta-synuclein rendered fibrillogenic by designed mutations.

Shahin Zibaee¹, Graham Fraser, Ross Jakes

¹Medical Research Council Laboratory of Molecular Biology, Cambridge CB2 0QH, United Kingdom.

The Journal of Biological Chemistry

|September 14, 2010

Summary

This summary is machine-generated.

Physicochemical properties of synucleins, not specific residues, drive filament formation in neurodegenerative diseases. Modifying these properties can make non-pathological proteins fibrillogenic, offering insights into disease mechanisms.

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Last Updated: Jun 8, 2026

Generation of Alpha-Synuclein Preformed Fibrils from Monomers and Use In Vivo

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Published on: June 2, 2019

Sequential Extraction of Soluble and Insoluble Alpha-Synuclein from Parkinsonian Brains

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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:

Filamentous α-synuclein inclusions are hallmarks of neurodegenerative diseases like Parkinson's.
β-synuclein, though homologous, doesn't form pathological inclusions.
Previous work suggested filament formation depends on global and local protein properties, not specific residues.

Purpose of the Study:

To investigate how intrinsic physicochemical properties of synucleins influence their fibrillogenic propensity.
To determine if β-synuclein can be made fibrillogenic by altering its physicochemical properties.
To elucidate the mechanisms underlying synuclein filament formation and its role in neurodegeneration.

Main Methods:

Engineered point mutations in β-synuclein to enhance global physicochemical properties (propensity, charge, hydrophilicity).
Engineered point mutations in β-synuclein to enhance local physicochemical properties (β-strand contiguity).
Assessed the fibrillogenic capacity of mutated β-synuclein variants.

Main Results:

β-synuclein was rendered fibrillogenic through targeted point mutations.
Enhancing global physicochemical properties and local β-strand contiguity independently or combined influenced fibril formation.
Findings support that synuclein fibrillogenesis is modulated by distinct yet overlapping physicochemical modalities.

Conclusions:

Intrinsic physicochemical properties of synucleins are critical determinants of their fibrillogenic potential.
Modulating these properties offers a pathway to understand and potentially target synucleinopathies.
The study provides insights into the molecular basis of α-synuclein aggregation in neurodegenerative diseases.