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Related Experiment Video

Updated: Jan 21, 2026

Detection of Aggregation-Prone Behavior in Mutant P53 V157F Breast Cancer Cells Using Multipoint Thioflavin T Fluorescence
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Detection of Aggregation-Prone Behavior in Mutant P53 V157F Breast Cancer Cells Using Multipoint Thioflavin T Fluorescence

Published on: December 30, 2025

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Detection of Aggregation-Prone Behavior in Mutant P53 V157F Breast Cancer Cells Using Multipoint Thioflavin T

Shao-I Chin1, Zi-Min Zeng2, Sih-Tong Chen3

  • 1School of Medicine, I-Shou University.

Journal of Visualized Experiments : Jove
|January 19, 2026
PubMed
Summary

The TP53 V157F mutation in breast cancer cells promotes protein aggregation, forming amyloid-like structures. This aggregation, detected by Thioflavin T staining, highlights a novel cancer mechanism.

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Area of Science:

  • Molecular Biology
  • Cancer Research
  • Biochemistry

Background:

  • The TP53 gene encodes the tumor suppressor p53, crucial for genomic stability.
  • TP53 mutations are prevalent in human cancers, potentially causing loss of tumor suppression or gain-of-function.
  • Some TP53 mutations can lead to prion-like aggregation.

Purpose of the Study:

  • To investigate the aggregation tendency of the p53 V157F mutation.
  • To compare p53 aggregation in Hs578T breast cancer cells (V157F mutation) versus MCF7 cells (wild-type p53).

Main Methods:

  • Utilized Thioflavin T (ThT) staining to detect protein aggregation.
  • Employed fluorescence quantification in 96-well plate assays using a microplate reader.
  • Performed both single-point and multipoint fluorescence readings for quantitative analysis.

Main Results:

  • Hs578T cells showed a 3.20- to 4.26-fold increase in ThT fluorescence compared to MCF7 cells.
  • Indicated significantly elevated levels of β-sheet-rich or amyloid-like aggregates in cells with the p53 V157F mutation.
  • Multipoint measurements confirmed consistent and widespread presence of protein aggregates.

Conclusions:

  • The p53 V157F mutation significantly enhances protein aggregation in breast cancer cells.
  • Thioflavin T staining combined with multipoint plate-reading is effective for detecting protein aggregation in cell-based assays.
  • Findings support a role for protein aggregation in the pathogenesis of TP53-mutated cancers.