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Updated: Sep 28, 2025

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

Rationally designed helical peptidomimetics disrupt α-synuclein fibrillation.

Clementine E Bavinton¹, Rebecca Sternke-Hoffmann², Tohru Yamashita³

¹School of Chemistry and the Institute for Life Sciences, University of Southampton, Southampton, SO17 1BJ, UK. st3a15@soton.ac.uk.

Chemical Communications (Cambridge, England)

|April 5, 2022

Summary

This summary is machine-generated.

Researchers developed peptidomimetics to target misfolded alpha-synuclein (α-Syn), a key factor in Parkinson's disease. These compounds slow aggregation and disrupt toxic fibril formation, offering potential therapeutic strategies.

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A Method to Study α-Synuclein Toxicity and Aggregation Using a Humanized Yeast Model

A Method to Study α-Synuclein Toxicity and Aggregation Using a Humanized Yeast Model

Published on: November 25, 2022

Area of Science:

Biochemistry
Neuroscience
Molecular Biology

Background:

Misfolding of alpha-synuclein (α-Syn) leads to toxic fibrils and Lewy bodies, characteristic of Parkinson's disease.
Understanding the structural basis of α-Syn misfolding is crucial for developing therapeutic interventions.

Purpose of the Study:

To design and utilize peptidomimetics for selective recognition of native helical α-Syn.
To investigate the potential of these peptidomimetics in inhibiting α-Syn aggregation and misfolding pathways.

Main Methods:

Rational design of peptidomimetics targeting charged and hydrophobic residues on the helical α-Syn surface.
Lipid-catalyzed aggregation assays using thioflavin-T.
Electron microscopy to visualize aggregate structures.
Circular dichroism spectroscopy for conformational analysis.

Main Results:

Peptidomimetics demonstrated the ability to slow the rate of α-Syn aggregation under lipid-catalyzed conditions.
Electron microscopy confirmed that the compounds disrupt the α-Syn misfolding pathway and aggregate formation.
Control compounds and spectroscopic data supported the hypothesis of selective recognition.

Conclusions:

A supramolecular approach using rationally designed peptidomimetics can effectively target and inhibit α-Syn misfolding.
These compounds show potential as tools to study structure-function relationships in Parkinson's disease pathogenesis, including missense mutations and amyloid polymorphism.