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, normally used to...

You might also read

Related Articles

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

Sort by

Same author

Distinctive characteristics of dopamine neuron release mechanisms: Insights into Parkinson's Disease.

Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie·2026

Same author

Spark or Sound: How Two Differing Explanatory Strategies Impact the Debate on the Physical Nature of Neuronal Excitability.

Membranes·2026

Same author

Hands-on practicals in pharmacology teaching at university level: Outpaced by computer-based simulations, or is there a (blended) future?

European journal of pharmacology·2025

Same author

Two scientific perspectives on nerve signal propagation: how incompatible approaches jointly promote progress in explanatory understanding.

History and philosophy of the life sciences·2024

Same author

Thinking about the action potential: the nerve signal as a window to the physical principles guiding neuronal excitability.

Frontiers in cellular neuroscience·2023

Same author

Cerebellar presence of immune cells in patients with neuro-coeliac disease.

Acta neuropathologica communications·2023

Search research articles

Related Experiment Video

Updated: Jul 4, 2026

Detection of Disease-associated α-synuclein by Enhanced ELISA in the Brain of Transgenic Mice Overexpressing Human A53T Mutated α-synuclein

Detection of Disease-associated α-synuclein by Enhanced ELISA in the Brain of Transgenic Mice Overexpressing Human A53T Mutated α-synuclein

Published on: May 30, 2015

Tissue transglutaminase modulates alpha-synuclein oligomerization.

Ine M J Segers-Nolten¹, Micha M M Wilhelmus, Gertjan Veldhuis

¹Biophysical Engineering Group, MESA+ Institute for Nanotechnology and Institute for Biomedical Technology, University of Twente, 7500 AE Enschede, The Netherlands.

Protein Science : a Publication of the Protein Society

|May 29, 2008

Summary

Tissue transglutaminase (tTG) effectively cross-links alpha-synuclein, preventing the formation of toxic fibrils implicated in Parkinson's disease. This interaction inhibits the development of pathogenic oligomeric species.

More Related Videos

Bioluminescence Imaging of Neuroinflammation in Transgenic Mice After Peripheral Inoculation of Alpha-Synuclein Fibrils

Bioluminescence Imaging of Neuroinflammation in Transgenic Mice After Peripheral Inoculation of Alpha-Synuclein Fibrils

Published on: April 13, 2017

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

Related Experiment Videos

Last Updated: Jul 4, 2026

Detection of Disease-associated α-synuclein by Enhanced ELISA in the Brain of Transgenic Mice Overexpressing Human A53T Mutated α-synuclein

Detection of Disease-associated α-synuclein by Enhanced ELISA in the Brain of Transgenic Mice Overexpressing Human A53T Mutated α-synuclein

Published on: May 30, 2015

Bioluminescence Imaging of Neuroinflammation in Transgenic Mice After Peripheral Inoculation of Alpha-Synuclein Fibrils

Bioluminescence Imaging of Neuroinflammation in Transgenic Mice After Peripheral Inoculation of Alpha-Synuclein Fibrils

Published on: April 13, 2017

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

Area of Science:

Biochemistry
Neuroscience
Protein Chemistry

Background:

Parkinson's disease is associated with alpha-synuclein protein variants.
Tissue transglutaminase (tTG) is an enzyme that forms cross-links between proteins.
Alpha-synuclein aggregation into fibrils and oligomers is central to Parkinson's pathology.

Purpose of the Study:

To investigate the interaction between tissue transglutaminase (tTG) and Parkinson's disease-associated alpha-synuclein.
To determine the binding affinity of tTG for wild-type and mutant alpha-synuclein.
To characterize the structural and functional properties of alpha-synuclein oligomers formed in the presence of tTG.

Main Methods:

Surface plasmon resonance (SPR) to measure binding affinities.
Atomic force microscopy (AFM) to visualize oligomer morphology.
Biochemical assays to assess oligomer stability and membrane disruption.

Main Results:

tTG binds wild-type and mutant alpha-synuclein with high affinity (nanomolar constants).
tTG effectively cross-links alpha-synuclein, inhibiting fibril formation and producing stable, unstructured oligomers.
These tTG-induced oligomers are resistant to denaturation and do not disrupt phospholipid vesicles.

Conclusions:

tTG interaction with alpha-synuclein prevents the formation of pathogenic, membrane-disrupting oligomers.
tTG-mediated cross-linking imposes structural constraints, blocking alpha-synuclein aggregation into toxic species.
Cross-linking amyloid-forming proteins like alpha-synuclein by tTG may be a therapeutic strategy against neurodegenerative diseases.