Polyglutamine Aggregation
Polyglutamine Aggregation - Related Videos
03:03
Fluorescent Reporter-Based Paralysis Assay: A Technique to Assess Age-Associated Progressive Formation of Polyglutamine Fluorescent Reporter and Associated Paralysis in Caenorhabditis elegans
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2025
This video demonstrates an in vivo imaging-based assay to determine proteostasis decline due to aging. The assay uses Caenorhabditis elegans expressing polyglutamine YFP-fusion protein in body wall muscles to measure the age-associated aggregation of polyglutamine and induction of proteotoxicity, leading to paralysis.
04:32
PolyQ Aggregation Assay to Identify Neuroprotective Effect of a Compound in Worms
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2025
This video describes an in vivo method to screen the protective potential of neuroprotective test compounds in reducing polyQ aggregation in body wall muscle cells of nematodes and ameliorating aggregation-associated proteotoxicity.
09:06
Growth Assays to Assess Polyglutamine Toxicity in Yeast
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Cited by 3 •
2012
This manuscript describes three complementary protocols for assessing the toxicity of polyglutamine (polyQ)-expansion proteins in the yeast Saccharomyces cerevisiae. These protocols can easily be modified to monitor the toxicity of other misfolded proteins in yeast.
10:10
Aggregates for Concrete and Asphaltic Mixes
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2023
Source: Roberto Leon, Department of Civil and Environmental Engineering, Virginia Tech, Blacksburg, VA Concrete and asphalt are by far the most common construction materials used today. Concrete is a composite material consisting of cement, water, air, coarse aggregate, and fine aggregates. Fine aggregates are typically sands and coarse aggregates are natural or crushed rocks. Chemical admixtures to modify certain specific properties are also commonly used (i.e., superplasticizers to make the...
09:23
Effect of Fluorescent Proteins on Fusion Partners Using Polyglutamine Toxicity Assays in Yeast
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Cited by 1 •
2018
This article describes protocols to assess the effect of fluorescent proteins on the aggregation and toxicity of misfolded polyglutamine expansion for the rapid evaluation of a newly uncharacterized fluorescent protein in the context of fluorescent reporters.
FAQs
Longer glutamine-rich sequences can destabilize the protein structure, leaving the protein more prone to abnormal intermolecular interactions. These interactions allow misfolded molecules to associate first into soluble oligomers and later into insoluble, amyloid-like fibrils. Tracking this progression helps researchers connect sequence expansion with the distinct aggregate species observed in cellular and biochemical studies.
Soluble oligomers and insoluble fibrils represent different assembly states, so measuring them separately gives a more precise picture of aggregation. Fluorescence assays, microscopy, and biochemical measurements can help characterize which species are present. This distinction is useful when evaluating how aggregate formation affects cells and when comparing strategies intended to reduce misfolding or promote aggregate clearance.
CAG repeat expansion generates longer polyglutamine tracts, which can increase structural instability and strengthen abnormal interactions between protein molecules. That sequence-dependent change supports assembly into oligomers and fibrils. Comparing proteins with different tract lengths therefore provides a way to examine how the underlying genetic expansion relates to aggregate formation and disease-associated cellular effects.
The process provides a model for examining how misfolded protein assemblies affect cells, including neurons affected in inherited neurodegenerative disorders. Researchers can relate the presence and form of aggregates to cellular outcomes while using biological assays to characterize those species. This approach helps clarify mechanisms associated with neuronal toxicity without treating every aggregate form as biologically equivalent.
A study can begin with a protein-expression system to produce the polyglutamine-containing material, followed by fluorescence assays, microscopy, or biochemical aggregation measurements. Each technique contributes a different type of evidence about aggregate formation and appearance. Using several approaches together strengthens characterization of soluble and insoluble species and their effects on cells.
Fluorescence assays provide a technique for monitoring or characterizing aggregation-related species in experimental samples. Their results can be considered alongside microscopy and biochemical measurements rather than interpreted in isolation. This combined strategy helps researchers assess whether a system contains detectable assembly products and supports comparisons among genetic, pharmacological, or molecular interventions.
Microscopy helps visualize aggregation-related structures or patterns in biological samples, complementing measurements that may not show where species occur. When paired with protein-expression systems and biochemical assays, it contributes spatial and structural context to the analysis. This is particularly useful for relating aggregate formation to cellular effects in models of neurodegenerative disease.
Researchers can apply expression systems, fluorescence assays, microscopy, and biochemical measurements to compare interventions that target different stages of the process. Genetic, pharmacological, and molecular strategies may be assessed for their ability to reduce misfolding or enhance aggregate clearance. The resulting measurements help determine whether an intervention changes aggregate abundance, form, or cellular effects.