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Amyloid Fibrils

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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,...

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Related Experiment Video

Updated: May 28, 2025

Exogenous Administration of Microsomes-associated Alpha-synuclein Aggregates to Primary Neurons As a Powerful Cell Model of Fibrils Formation

Exogenous Administration of Microsomes-associated Alpha-synuclein Aggregates to Primary Neurons As a Powerful Cell Model of Fibrils Formation

Published on: June 26, 2018

Factors responsible for alpha-Synuclein aggregation.

Khuraijam Surjalal Singh¹, Rahul Verma², Nagendra Singh¹

¹Gautam Buddha University, Greater Noida, Gautam Budh Nagar, Uttar Pradesh, India.

Progress in Molecular Biology and Translational Science

|February 13, 2025

Summary

This summary is machine-generated.

Alpha-synuclein (α-Syn) aggregation is key in Parkinson's disease. Understanding factors influencing α-Syn misfolding and aggregation is crucial for developing effective Parkinson's disease therapies.

Keywords:

Aggregation Mutations Osmolytes Post-translational modifications α-Synuclein

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Last Updated: May 28, 2025

Exogenous Administration of Microsomes-associated Alpha-synuclein Aggregates to Primary Neurons As a Powerful Cell Model of Fibrils Formation

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Published on: June 26, 2018

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

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Published on: November 25, 2022

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

Area of Science:

Neuroscience
Biochemistry
Molecular Biology

Background:

Alpha-synuclein (α-Syn) aggregation into fibrils is a pathological hallmark of Parkinson's disease (PD).
Abnormal α-Syn forms, including oligomers and fibrils, drive neurodegeneration via mitochondrial and lysosomal dysfunction, and disrupted calcium homeostasis.
Structurally, α-Syn is an intrinsically disordered protein with distinct domains influencing its aggregation propensity.

Purpose of the Study:

To provide an elaborate explanation of factors influencing the structure, function, and aggregation of α-Syn.
To elucidate the mechanisms underlying α-Syn misfolding and aggregation in neurodegenerative disorders.
To highlight the importance of studying these factors for understanding PD pathogenesis and developing therapeutic strategies.

Main Methods:

Review and synthesis of existing literature on α-Syn structure, function, and aggregation.
Analysis of factors including protein expression, mutations, posttranslational modifications, and molecular interactions.
Exploration of the structural transitions of α-Syn from random coil to β-sheet rich structures.

Main Results:

α-Syn aggregation is influenced by high protein expression, genetic mutations, and posttranslational modifications.
Interactions with small molecules like osmolytes can modulate α-Syn aggregation.
The intrinsically disordered nature of α-Syn and its structural transformation upon lipid binding are critical to its aggregation pathway.

Conclusions:

Understanding the factors driving α-Syn misfolding and aggregation is essential for deciphering PD pathophysiology.
Investigating these mechanisms offers potential for identifying novel therapeutic targets for Parkinson's disease.
Detailed study of α-Syn behavior provides insights into selective neuronal atrophy in α-Syn-related neurodegenerative disorders.