Aggregation-prone Proteins
Aggregation-prone Proteins - Related Videos
09:22
In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein
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Cited by 21 •
2015
Unmodified and hyperphosphorylated tau proteins were used in two in vitro aggregation assays to reveal the hyperphosphorylation-dependent fast aggregation kinetics. These assays pave the way for future screens for compounds that can modulate the propensity of hyperphosphorylated tau to form fibrils that underlie the progression of Alzheimer’s disease.
11:57
Methods to Study Changes in Inherent Protein Aggregation with Age in Caenorhabditis elegans
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Cited by 7 •
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.
05:42
Misfolding-Prone Protein Degradation Assay: A Technique to Monitor Misfolded Protein Degradation Using Cycloheximide Treatment and Detergent Fractionation
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2025
This video describes a degradation assay for misfolded proteins using cycloheximide treatment along with detergent fractionation. This method aids in studying the dynamics of misfolded proteins and uncovering the in-depth mechanisms of protein turnover.
04:12
Protein Aggregate Formation Assay: A Method to Detect and Quantify Protein Aggregation in Cultured Cells upon Induction by Proteasome Inhibitor
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2025
In this video, we demonstrate a cell-based protein aggregation assay using proteasome inhibitors, which block proteasome activity, preventing misfolded, mutant proteins, fused to a fluorescent label, from undergoing ubiquitin-dependent proteasomal degradation, leading to their accumulation within the cell cytoplasm. The protein aggregates are then visualized and quantified by fluorescence microscopy.
04:56
Detection of Aggregation-Prone Behavior in Mutant P53 V157F Breast Cancer Cells Using Multipoint Thioflavin T Fluorescence
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2025
Hs578T breast cancer cells harboring the p53 V157F mutation exhibit significantly higher Thioflavin T fluorescence compared to MCF7 cells, indicating enhanced protein aggregation. Multipoint fluorescence measurements improve detection accuracy and reliability in identifying β-sheet-rich aggregates, underscoring the importance of aggregation-prone p53 mutations in cancer research and the development of therapeutic strategies.
FAQs
Sequence changes or altered folding conditions can destabilize a protein and expose hydrophobic regions that are normally buried inside its structure. Higher concentration and cellular stress can increase opportunities for these exposed surfaces to interact between molecules. Those intermolecular contacts shift the balance toward association, allowing early assemblies to accumulate and progress into larger deposits.
Soluble oligomers and mature aggregates represent different stages or forms of protein assembly. Oligomers remain comparatively small and soluble, whereas fibrils or amorphous deposits are larger, less soluble structures. Separating these states helps researchers determine how aggregation progresses and identify which assemblies are associated with disrupted protein homeostasis or cellular impairment.
Molecular chaperones and degradation pathways act as cellular quality-control systems that limit the accumulation of misfolded or assembled proteins. Chaperones can help manage improperly folded species, while degradation pathways remove proteins that cannot be maintained safely. Studying both responses shows how cells preserve proteostasis and what happens when these safeguards become insufficient.
A useful comparison considers protein sequence, folding conditions, concentration, and cellular stress because each can alter exposure of hydrophobic regions and the likelihood of intermolecular association. Researchers can then examine whether the resulting material remains soluble or forms oligomers, fibrils, or amorphous deposits. This approach connects initiating conditions with the physical state of the assemblies produced.
These proteins provide experimental models for examining protein folding, cellular quality control, and the maintenance of protein homeostasis. By following how misfolded species associate and how cells respond, investigators can study the relationship between molecular assembly and cellular impairment. The same models also support research into aggregation-associated disease and strategies intended to prevent harmful accumulation.
Aggregation studies can reveal how failures in protein homeostasis allow abnormal assemblies to persist, increase, or interfere with cellular function. Comparing soluble intermediates with mature deposits helps link specific assembly states to cellular consequences rather than treating all aggregates as equivalent. This context informs efforts to understand aggregation-associated disease and evaluate ways to limit harmful protein accumulation.