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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,...

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Related Experiment Video

Updated: Oct 17, 2025

Imaging the Intracellular Trafficking of APP with Photoactivatable GFP

Imaging the Intracellular Trafficking of APP with Photoactivatable GFP

Published on: October 17, 2015

The cellular modifier MOAG-4/SERF drives amyloid formation through charge complementation.

Anita Pras¹, Bert Houben^2,3, Francesco A Aprile⁴

¹European Research Institute for the Biology of Ageing, University of Groningen, University Medical Centre Groningen, Groningen, The Netherlands.

The EMBO Journal

|October 7, 2021

Summary

This summary is machine-generated.

Cellular proteins MOAG-4 and SERF2 accelerate aging and disease by promoting protein aggregation. Neutralizing charge interactions with these proteins suppressed aggregation and toxicity, revealing a potential therapeutic target.

Keywords:

MOAG-4 SERF amyloid protein aggregation protein quality control

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Last Updated: Oct 17, 2025

Imaging the Intracellular Trafficking of APP with Photoactivatable GFP

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Assay Development for High Content Quantification of Sod1 Mutant Protein Aggregate Formation in Living Cells

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Published on: October 4, 2017

Area of Science:

Molecular Biology
Aging Research
Biochemistry

Background:

Protein aggregation is linked to aging and neurodegenerative diseases.
Cellular modifiers like MOAG-4 and SERF2 influence protein aggregation and toxicity.
The precise mechanisms of proteotoxicity remain incompletely understood.

Purpose of the Study:

To elucidate the cellular mechanisms underlying proteotoxicity mediated by aggregation-prone proteins.
To investigate the role of MOAG-4 and SERF2 in protein aggregation and age-related diseases.
To identify potential therapeutic targets for reducing age-related protein toxicity.

Main Methods:

Peptide array screening of human amyloidogenic proteins to identify interaction sites with SERF2.
Biochemical assays to assess the impact of charge neutralization on SERF2's amyloid-promoting activity.
Genetic manipulation in Caenorhabditis elegans models to study the in vivo effects of MOAG-4 charge neutralization on protein aggregation and toxicity.

Main Results:

SERF2 specifically interacts with negatively charged and hydrophobic aromatic amino acid segments in aggregation-prone proteins.
Eliminating these interaction sites or neutralizing positive charges on SERF2 abolished its amyloid-promoting activity.
Mutating the MOAG-4 locus to neutralize charge significantly suppressed protein aggregation and toxicity in C. elegans models.
These findings indicate that charge interactions between cellular modifiers and aggregation-prone proteins drive proteotoxicity.

Conclusions:

MOAG-4 and SERF2 promote protein aggregation and toxicity through charge-based interactions with aggregation-prone proteins.
These charge interactions may accelerate amyloid nucleation by altering protein structure and reducing colloidal stability.
Targeting these charge interactions presents a promising strategy for therapeutic interventions against age-related protein toxicity.