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Updated: Jul 10, 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

Phenylalanine-based fibrillar systems.

Soumen Kuila¹, Sukantha Dey¹, Pijush Singh^1,2

¹Department of Chemistry, University of North Bengal, Raja Rammohanpur, Siliguri 734013, West Bengal, India. jayanta@nbu.ac.in.

Chemical Communications (Cambridge, England)

|November 21, 2023

Summary

Phenylketonuria (PKU) involves phenylalanine (Phe) forming toxic amyloid fibrils, leading to intellectual disability. This review details Phe fibril formation, its toxicity, and inhibition strategies, offering a database against PKU.

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Area of Science:

Biochemistry
Neuroscience
Molecular Biology

Background:

Phenylketonuria (PKU) is a metabolic disorder caused by phenylalanine accumulation.
Excess phenylalanine forms toxic amyloid fibrils, contributing to neurodegeneration.
Understanding fibril formation is crucial for developing PKU therapies.

Purpose of the Study:

To review the formation of phenylalanine-based amyloid fibrils.
To discuss the factors influencing fibril formation kinetics.
To explore inhibition strategies and compare toxicity with other neurodegenerative peptides.

Main Methods:

Literature review of Phe fibril formation studies.
Analysis of spectroscopic and microscopic techniques for self-assembly.
Comparison of Phe-fibril toxicity with other amyloidogenic peptides.

Main Results:

Fibril formation is influenced by solvent, pH, concentration, and temperature.
Phe-based fibrils exhibit toxicity and can induce other proteins to form fibrils.
Various compounds, including polyphenols, drugs, and nanoparticles, inhibit fibril formation.

Conclusions:

Phe fibril formation is a complex process influenced by multiple factors.
Inhibiting Phe fibril formation is a promising therapeutic strategy for PKU.
This work provides a comprehensive database for PKU research and therapeutic development.