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Updated: Jul 11, 2026
05:48
Rapid Generation of Amyloid from Native Proteins In vitro
Published on: December 5, 2013
Amyloid peptides and proteins in review
R S Harrison1, P C Sharpe, Y Singh
1Centre for Drug Design and Development, Institute for Molecular Bioscience, University of Queensland, QLD 4072, Brisbane, Australia.
Reviews of Physiology, Biochemistry and Pharmacology
|September 12, 2007
Summary
Amyloids are protein deposits linked to diseases like Alzheimer's and diabetes. Research explores their structure, formation, and role in both pathology and normal physiology, challenging disease-only associations.
Area of Science:
- Biochemistry
- Molecular Biology
- Pathology
Background:
- Amyloids are protein aggregates implicated in over 30 diseases, including neurodegenerative and systemic conditions.
- Protein misfolding and aggregation into beta-sheet structures are key features of amyloid diseases.
- Recent findings suggest intermediate aggregated states, not just insoluble polymers, may cause cellular toxicity.
Purpose of the Study:
- To summarize current knowledge on amyloidogenic peptides and proteins.
- To explore the occurrence, structure, folding pathways, chemistry, and biology of amyloids.
- To highlight factors influencing amyloid formation (amyloidogenesis).
Main Methods:
- Review of existing literature on amyloid formation and associated diseases.
- Analysis of in vitro studies on amyloidogenic peptides.
- Identification and characterization of non-pathological amyloidogenic proteins.
Main Results:
- Amyloids are filamentous protein deposits with diverse roles.
- Alpha-helix to beta-sheet transitions are implicated in amyloid formation.
- Non-pathological amyloids with physiological functions have been identified, broadening the understanding beyond disease.
Conclusions:
- Amyloid formation is a complex process influenced by various factors.
- Amyloids are not exclusively associated with disease; some have normal physiological roles.
- Further research is needed to fully understand the mechanisms and implications of amyloidogenesis.
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