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Updated: Nov 11, 2025
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Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast
Published on: June 23, 2018
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The seesaw between normal function and protein aggregation: How functional interactions may increase protein
Piero Andrea Temussi1, Gian Gaetano Tartaglia2,3, Annalisa Pastore1
1UK Dementia Research Institute at King's College London, The Maurice Wohl Institute, London, UK.
Summary
Protein aggregation may occur due to the absence of natural chaperone partners. Targeting these partners offers a novel strategy for developing anti-aggregation therapies for protein misfolding diseases.
Area of Science:
- Biochemistry
- Molecular Biology
- Structural Biology
Background:
- Protein aggregation is a known phenomenon studied for decades.
- Existing principles of protein aggregation are well understood.
- Functional protein surfaces are implicated in aggregation.
Purpose of the Study:
- To propose a novel perspective on protein aggregation.
- To hypothesize that aggregation is a side-effect of lacking natural chaperone partners.
- To suggest a new therapeutic strategy for protein aggregation diseases.
Main Methods:
- Review of existing literature on protein aggregation.
- Analysis of paradigmatic examples supporting the hypothesis.
- Theoretical substantiation of the proposed mechanism.
Main Results:
- Protein aggregation may result from the absence of physiological chaperone partners.
- Functional protein surfaces, when unbound, can promote aggregation.
- Three examples support the generality of this hypothesis.
Conclusions:
- The lack of natural partners acting as chaperones can drive protein aggregation.
- Targeting these physiological partners is a direct approach for anti-aggregation molecule design.
- This perspective offers a new strategy for combating protein aggregation and misfolding diseases.
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