ArticleCellular and molecular life sciences : CMLS2018
Amyloid and the origin of life: self-replicating catalytic amyloids as prebiotic informational and protometabolic entities.
Article in Cellular and molecular life sciences : CMLS, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 108 citations in OpenAlex.
- Functional abiotic metabolite assembly hypothesis for the early events in the origin of life.Nature communications · 2026Review
- Conserved catalytic motifs encode enzyme-like supramolecular peptide assemblies.Research square · 2026Article
- Conditions Enabling the Persistence of Cooperating Synthetase, Ligase, and Mutation-Inhibitor Catalytic Polymers.Journal of molecular evolution · 2026Article
- Enzymes of physiological amyloidogenesis control pathological amyloid toxicity.Life science alliance · 2026Article
- Catalytic Amyloids: Turning Fibrils Into Biocatalysts.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Review
- Structure-activity relationships in catalytic amyloids.Journal of inorganic biochemistry · 2026Article
- Prebiotically Plausible Peptides can Self-assemble into β-rich Nanostructures.bioRxiv : the preprint server for biology · 2025Article
- Surface properties of lysozyme aqueous solutions in the presence of reducing agents: The effect of disulfide bonds reshuffling.Biophysical journal · 2025Article
- Origin of life: β-sheet amyloid conformers as the primordial functional polymers on the early Earth and their role in the emergence of complex dynamic networks.FEBS letters · 2025Review
- The Influence of POPC as a Coaggregate in Amyloid-β Oligomer Formation.ACS chemical neuroscience · 2025Article
- The role of hydrophobic collapse in cytotoxic and functional amyloid oligomerization.Biophysical journal · 2025Article
- Valorization of Baltic Sea farmed blue mussels: Chemical profiling and prebiotic potential for nutraceutical and functional food development.Food chemistry: X · 2024Article
- The prebiotic emergence of biological evolution.Royal Society open science · 2024Article
- Emergence of a short peptide based reductase via activation of the model hydride rich cofactor.Nature communications · 2024Article
- Review
- Discovery and application of food catalysts to promote the coupling of PQQ (quinone) with amines.Frontiers in nutrition · 2024Article
- An Analysis of Nucleotide-Amyloid Interactions Reveals Selective Binding to Codon-Sized RNA.Journal of the American Chemical Society · 2023Article
- Eco-evolutionary trade-offs in the dynamics of prion strain competition.Proceedings. Biological sciences · 2023Article
- Cascade autohydrolysis of Alzheimer's Aβ peptides.Chemical science · 2023Article
- A Comprehensive Analysis of the Intrinsic Visible Fluorescence Emitted by Peptide/Protein Amyloid-like Assemblies.International journal of molecular sciences · 2023Review
Corrections and comments
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1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A crucial stage in the origin of life was the emergence of the first molecular entity that was able to replicate, transmit information, and evolve on the early Earth. The amyloid world hypothesis posits that in the pre-RNA era, information processing was based on catalytic amyloids. The self-assembly of short peptides into β-sheet amyloid conformers leads to extraordinary structural stability and novel multifunctionality that cannot be achieved by the corresponding nonaggregated peptides. The new functions include self-replication, catalytic activities, and information transfer. The environmentally sensitive template-assisted replication cycles generate a variety of amyloid polymorphs on which evolutive forces can act, and the fibrillar assemblies can serve as scaffolds for the amyloids themselves and for ribonucleotides proteins and lipids. The role of amyloid in the putative transition process from an amyloid world to an amyloid-RNA-protein world is not limited to scaffolding and protection: the interactions between amyloid, RNA, and protein are both complex and cooperative, and the amyloid assemblages can function as protometabolic entities catalyzing the formation of simple metabolite precursors. The emergence of a pristine amyloid-based in-put sensitive, chiroselective, and error correcting information-processing system, and the evolvement of mutualistic networks were, arguably, of essential importance in the dynamic processes that led to increased complexity, organization, compartmentalization, and, eventually, the origin of life.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.