Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

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,...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Atg18 interaction positions Atg2 for efficient lipid transfer into phagophore elongation.

The EMBO journal·2026

Same author

Seeing Invisible Oligomers: Rethinking α-Synuclein Pathology Through Proximity Ligation Assay.

Movement disorders : official journal of the Movement Disorder Society·2026

Same author

A dual sensor regulates P-glycoprotein's structural plasticity.

bioRxiv : the preprint server for biology·2026

Same author

A Salt Bridge Pre-arranges the Structure of the ABC Transporter BmrA for Proper NBD Dimerization.

Journal of molecular biology·2026

Same author

Higher-molecular-weight a-synuclein oligomers are increased in the brain cytosol of patients with dementia with Lewy bodies.

NPJ Parkinson's disease·2026

Same author

Paediatric, age-specific reference intervals for reticulocyte count on Abbotts Alinity hq platform.

Scandinavian journal of clinical and laboratory investigation·2025

Search research articles

Related Experiment Video

Updated: Jan 5, 2026

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

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

Published on: January 5, 2016

Stabilization of α-synuclein oligomers using formaldehyde.

Harm Ruesink^1,2, Lasse Reimer^1,2, Emil Gregersen^1,2

¹Danish Research Institute of Translational Neuroscience-DANDRITE, Aarhus University, Aarhus, Denmark.

|October 12, 2019

Summary

Researchers stabilized alpha-synuclein (α-syn) oligomers, crucial for Parkinson's disease research, using formaldehyde. These stabilized oligomers serve as reliable biomarkers for synucleinopathies.

More Related Videos

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

Preparation of Oligomeric β-amyloid1-42 and Induction of Synaptic Plasticity Impairment on Hippocampal Slices

Preparation of Oligomeric β-amyloid1-42 and Induction of Synaptic Plasticity Impairment on Hippocampal Slices

Published on: July 14, 2010

Related Experiment Videos

Last Updated: Jan 5, 2026

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

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

Published on: January 5, 2016

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

Preparation of Oligomeric β-amyloid1-42 and Induction of Synaptic Plasticity Impairment on Hippocampal Slices

Preparation of Oligomeric β-amyloid1-42 and Induction of Synaptic Plasticity Impairment on Hippocampal Slices

Published on: July 14, 2010

Area of Science:

Neuroscience
Biochemistry
Molecular Biology

Background:

Neurodegenerative diseases like Parkinson's disease (PD), dementia with Lewy bodies (DLB), and multiple system atrophy (MSA) are characterized by alpha-synuclein (α-syn) aggregates.
Soluble α-syn oligomers are hypothesized intermediates in aggregation and potential biomarkers for synucleinopathies.
The instability of α-syn oligomers prepared in vitro complicates research and biomarker development.

Purpose of the Study:

To develop a method for stabilizing α-syn oligomers.
To ensure stabilized oligomers retain their structural and antigenic properties.
To validate the utility of stabilized oligomers as reliable standards in biomarker assays.

Main Methods:

Utilized formaldehyde (FA), a small amine-reactive cross-linker, to stabilize α-syn oligomers.
Assessed the size, overall structure, and antigenicity of cross-linked oligomers using specific antibodies (FILA, MJFR-14-6-4-2).
Evaluated the stability of cross-linked oligomers against denaturants (urea, SDS) and their functionality as internal standards in ELISA.

Main Results:

Formaldehyde successfully stabilized α-syn oligomers without altering their size, structure, or antigenicity.
Cross-linked α-syn oligomers demonstrated resistance to urea and SDS treatment.
Stabilized oligomers remained functional as internal standards in aggregation-specific ELISA, even after urea exposure.

Conclusions:

FA-cross-linked α-syn oligomers provide a stable and reliable format for research.
These stabilized oligomers can serve as crucial calibrators for standardized biomarker studies in synucleinopathies.
This stabilization method facilitates comparative analysis and enhances the accuracy of α-syn biomarker quantification.