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

Gpnmb defines a phagocytic state of microglia linked to cell death in prion disease mouse model.

Nature communications·2026

Same author

Reduced plasma TIA-1: bridging established pathology and novel biomarker potential.

Alzheimer's research & therapy·2026

Same author

A distinct tau oligomer strain defines the molecular and proteomic landscape of rapidly progressive Alzheimer's disease.

Acta neuropathologica·2026

Same author

Detection of alpha-synuclein seeding activity in tear fluid in patients with Parkinson's disease.

NPJ Parkinson's disease·2026

Same author

Therapeutic Potential of Amyloid-β Interactors in Rapidly Progressive Alzheimer's Disease-An In Silico Study.

Molecular informatics·2026

Same author

Alterations in cerebrospinal fluid levels of myelin- and oligodendrocyte-related proteins in sporadic Creutzfeldt-Jakob disease.

Acta neuropathologica communications·2026

Search research articles

Related Experiment Video

Updated: May 7, 2026

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

Published on: January 2, 2015

Alpha-Synuclein Demonstrates Varying Binding Affinities With Different Tau Isoforms.

Anna-Lisa Fischer¹, Matthias Schmitz¹, Tobias Thom¹

¹Department of Neurology, University Medical Center Göttingen and the German Center for Neurodegenerative Diseases (DZNE), Göttingen, Germany.

Journal of Neurochemistry

|April 1, 2025

Summary

Alpha-synuclein (aSyn) and tau proteins directly interact, with binding affinity varying by tau isoform. This interaction occurs intracellularly and is crucial for understanding mixed-pathology neurodegenerative diseases like Alzheimer's and Parkinson's.

Keywords:

Alzheimer's disease Parkinson's disease alpha‐synuclein interaction synucleinopathies tau tauopathies

More Related Videos

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

In Vitro Assay for Studying the Aggregation of Tau Protein and Drug Screening

In Vitro Assay for Studying the Aggregation of Tau Protein and Drug Screening

Published on: November 20, 2018

Related Experiment Videos

Last Updated: May 7, 2026

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

Published on: January 2, 2015

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

In Vitro Assay for Studying the Aggregation of Tau Protein and Drug Screening

In Vitro Assay for Studying the Aggregation of Tau Protein and Drug Screening

Published on: November 20, 2018

Area of Science:

Neuroscience
Biochemistry
Cell Biology

Background:

Neurodegenerative diseases are characterized by protein aggregation, including amyloid-beta, tau, and alpha-synuclein (aSyn).
Mixed pathologies, involving co-existing protein aggregates like aSyn and tau, are common in diseases such as Alzheimer's and synucleinopathies.
The potential interaction and crosstalk between misfolded aSyn and tau remain incompletely understood.

Purpose of the Study:

To investigate the direct binding characteristics between monomeric alpha-synuclein (aSyn) and different tau isoforms.
To examine the potential co-localization of aSyn and tau within cells.
To elucidate the significance of aSyn-tau interactions in the context of mixed-pathology neurodegenerative diseases.

Main Methods:

Surface Plasmon Resonance (SPR) spectroscopy was employed to quantify direct protein-protein interactions and binding kinetics between aSyn and tau isoforms.
SH-SY5Y cells were utilized for co-localization studies to observe the intracellular presence of aSyn and tau together.
Subcellular fractionation was performed to determine the cellular compartments where aSyn and tau co-localize.

Main Results:

SPR analysis revealed direct binding between aSyn and tau isoforms, with varying affinities.
The strongest binding affinity was observed between aSyn and the 1N3R tau isoform, followed by 2N3R and 2N4R tau isoforms.
Co-localization studies demonstrated that aSyn and all tested tau isoforms were found within the same cellular compartments, including membrane, nuclear, and cytoskeletal fractions.

Conclusions:

Alpha-synuclein (aSyn) and tau are direct interaction partners, with binding affinity influenced by specific tau isoforms.
Intracellular co-localization of aSyn and tau in various cellular compartments suggests a significant interplay.
These findings are critical for understanding the pathophysiology of neurodegenerative diseases with mixed pathologies and may inform therapeutic strategies.