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Updated: Sep 29, 2025
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Rapid Generation of Amyloid from Native Proteins In vitro
Published on: December 5, 2013
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Amyloid Cross-Seeding: Mechanism, Implication, and Inhibition.
Sushma Subedi1, Santanu Sasidharan2, Niharika Nag1
1Molecular and Structural Biophysics Laboratory, Department of Biochemistry, North-Eastern Hill University, Shillong 793022, India.
Molecules (Basel, Switzerland)
|March 26, 2022
Summary
Neurodegenerative diseases stem from misfolded protein aggregates. Targeting common epitopes in cross-seeding amyloid proteins offers a promising therapeutic strategy for these conditions.
Area of Science:
- Biochemistry
- Neuroscience
- Pathology
Background:
- Neurodegenerative diseases like Alzheimer's and Parkinson's are linked to misfolded protein aggregates.
- These aggregates form through homologous or heterologous sequence interactions.
- Amyloid protein cross-seeding, leading to multicomponent assemblies, is observed but poorly understood at a molecular level.
Purpose of the Study:
- To provide a detailed discussion of amyloid proteins and cross-seeding phenomena.
- To explore the potential of targeting common epitopes in cross-seeding amyloid proteins.
- To examine dual inhibitors for amyloid proteins involved in cross-seeding.
Main Methods:
- Literature review and discussion of existing experimental evidence.
- Analysis of data suggesting therapeutic strategies.
- Examination of dual inhibitor mechanisms.
Main Results:
- Cross-seeding of amyloid proteins leads to multicomponent assemblies.
- Targeting common epitopes of interacting amyloid proteins may be more effective than single-target approaches.
- Dual inhibitors offer a potential therapeutic avenue.
Conclusions:
- Understanding amyloid cross-seeding is crucial for developing effective anti-amyloid therapeutics.
- Targeting common epitopes and utilizing dual inhibitors are promising strategies.
- Further research is needed to address challenges in mechanism elucidation and therapeutic design.
