Related Experiment Video

Updated: Aug 15, 2025

A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis
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A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis

Published on: May 22, 2018

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The role of heat shock proteins in preventing amyloid toxicity

Ricarda Törner1, Tatsiana Kupreichyk2,3, Wolfgang Hoyer2,3

  • 1University Grenoble Alpes, CNRS CEA Institut de Biologie Structurale (IBS), Grenoble, France.

Frontiers in Molecular Biosciences
|January 2, 2023
PubMed

Insights

Aging increases amyloid fibril formation and cellular toxicity. This review overviews how molecular chaperones, key to protein quality control, counteract amyloidogenic proteins, highlighting current research and future directions.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Protein misfolding and aggregation into amyloid fibrils are linked to aging and cellular toxicity.
  • Cellular quality control systems, including chaperones, decline with age, exacerbating protein aggregation.
  • Chaperones are crucial for maintaining protein homeostasis and preventing the accumulation of toxic protein species.

Purpose of the Study:

  • To provide a comprehensive overview of the interplay between chaperones and amyloidogenic proteins.
  • To summarize recent advances in understanding how chaperones modulate protein conformational states and prevent amyloid toxicity.
  • To highlight challenges and open questions in the field of chaperone-mediated amyloid regulation.

Main Methods:

  • Review of structural and mechanistic studies on chaperones and amyloidogenic proteins.
  • Analysis of research focusing on the modulatory effects of chaperones on protein aggregation.
  • Synthesis of findings from investigations into the functional interactions between chaperones and amyloidogenic proteins.

Main Results:

  • Chaperones play a critical role in preventing the formation and toxicity of amyloid fibrils.
  • Understanding chaperone mechanisms provides insights into age-related proteinopathies.
  • Structural and functional studies reveal specific interactions that can be targeted for therapeutic interventions.

Conclusions:

  • Chaperones are key regulators of protein homeostasis, with significant implications for age-related diseases.
  • Further research into chaperone-amyloid interactions is essential for developing novel therapeutic strategies.
  • This review serves as a foundational resource for researchers entering the field of protein aggregation and quality control.
Keywords:
HSPaggregationamyloidchaperonesstructural biology

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