Polyq Aggregation
Polyq Aggregation - Related Videos
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.
05:36
Fluorescence Lifetime Imaging of PolyQ Protein Aggregation in Caenorhabditis elegans Neurons
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2025
Source: Pigazzini, M. L., et. al. Characterization of Amyloid Structures in Aging C. Elegans Using Fluorescence Lifetime Imaging. J. Vis. Exp. (2020).This video demonstrates the use of fluorescence lifetime imaging microscopy (FLIM) to assess polyQ protein aggregation in C. elegans neurons, comparing control and chaperone protein-deficient worms. Increased aggregation in chaperone-deficient worms promotes energy transfer between clustered fluorophores, reducing fluorescence lifetime.
04:06
An Assay to Study Effect of Test Compound against PolyQ-Mediated Neurotoxicity in Worms
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2025
In this video, we describe a method to evaluate the neuroprotective effect of a test compound, astragalan, on neuronal survival in Caenorhabditis elegans from polyQ-mediated neurotoxicity. The assay uses Caenorhabditis elegans expressing the abnormally expanded polyQ repeats fused to GFP in their ASH neurons to measure neuronal survival following test compound treatment.
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...
11:57
Methods to Study Changes in Inherent Protein Aggregation with Age in Caenorhabditis elegans
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Cited by 6 •
2017
The goal of the method presented here is to explore protein aggregation during normal aging in the model organism C. elegans. The protocol represents a powerful tool to study the highly insoluble large aggregates that form with age and to determine how changes in proteostasis impact protein aggregation.
FAQs
Expanded glutamine stretches can destabilize the structure of the protein that carries them, exposing aggregation-prone features. Glutamine residues then support intermolecular hydrogen bonding, allowing separate protein molecules to associate. This molecular combination shifts the system from normally soluble proteins toward assemblies that can progress through oligomeric and fibrillar forms, providing a mechanistic link between repeat expansion and abnormal protein accumulation.
These assemblies represent distinct physical states along the aggregation process. Soluble oligomers are relatively small associated species, whereas amyloid-like fibrils are insoluble, elongated assemblies formed in many cases. Intracellular inclusions are accumulation sites within cells that may contain aggregated material. Distinguishing these forms helps researchers examine whether cellular effects accompany early soluble assemblies, later fibrils, or concentrated inclusions.
Repeat expansion can change the behavior and structural stability of proteins in ways that promote abnormal assemblies inside neurons. The resulting burden is relevant because neurons are the cells affected in disorders such as Huntington’s disease and several spinocerebellar ataxias. Studying this connection allows researchers to relate molecular aggregation states to broader disruption of neuronal function and survival.
Experimental models provide systems for following the formation of polyglutamine assemblies and examining how cells respond to them. They can be used to study protein quality control, cellular clearance pathways, and the appearance of aggregation-associated biomarkers. These models also create a framework for testing strategies intended to prevent or reduce toxic protein assemblies, linking molecular observations with disease-relevant outcomes.
Tracking soluble oligomers, insoluble amyloid-like fibrils, and intracellular inclusions can reveal how aggregation progresses and which forms accumulate under particular conditions. This information supports the search for disease biomarkers and helps define the assemblies most relevant to cellular disruption. It also gives researchers measurable outcomes for evaluating approaches aimed at reducing or preventing harmful protein accumulation.
Polyglutamine aggregation is particularly relevant to inherited neurodegenerative disorders caused by genetic repeat expansions. Huntington’s disease and several spinocerebellar ataxias provide disease contexts in which researchers examine how expanded protein sequences relate to neuronal dysfunction and loss. Comparing these conditions helps place aggregation within a broader biology of protein quality control, cellular clearance, and disease progression.