ArticleInternational journal of molecular sciences2023
Amyloids of α-Synuclein Promote Chemical Transformations of Neuronal Cell Metabolites.
Article in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 18 citations in OpenAlex.
- Catalytic Amyloids: Turning Fibrils Into Biocatalysts.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Review
- Alpha-synuclein amyloids catalyze the degradation of ATP and other nucleotides.Scientific reports · 2025Article
- Role of iron in brain development, aging, and neurodegenerative diseases.Annals of medicine · 2025Review
- From Pathology to Materials Science and Engineering: Harnessing the Amyloid State for Biotechnological Applications.ACS applied materials & interfaces · 2025Review
- ATP Hydrolysis by α-Synuclein Amyloids is Mediated by Enclosing β-Strand.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Microbiota-Derived Tryptophan Metabolite Indole-3-Propionic Acid-Emerging Role in Neuroprotection.Molecules (Basel, Switzerland) · 2025Review
- In silico identification of substrate-binding sites in type-1A α-synuclein amyloids.Biophysical journal · 2025Article
- Allosteric amyloid catalysis by coiled coil fibrils.Nature communications · 2025Article
- Concomitant Pathologies and Their Impact on Parkinson Disease: A Narrative Overview of Current Evidence.International journal of molecular sciences · 2025Review
- Biological Amyloids Chemically Damage DNA.ACS chemical neuroscience · 2025Article
- Association between Parkinson's Disease and Cancer: New Findings and Possible Mediators.International journal of molecular sciences · 2024Review
- Chemical catalysis by biological amyloids.Biochemical Society transactions · 2023Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The assembly of α-synuclein into cross-β structured amyloid fibers results in Lewy body deposits and neuronal degeneration in Parkinson's disease patients. As the cell environment is highly crowded, interactions between the formed amyloid fibers and a range of biomolecules can occur in cells. Although amyloid fibers are considered chemically inert species, recent in vitro work using model substrates has shown α-synuclein amyloids, but not monomers, to catalyze the hydrolysis of ester and phosphoester bonds. To search for putative catalytic activity of α-synuclein amyloids on biologically relevant metabolites, we here incubated α-synuclein amyloids with neuronal SH-SY5Y cell lysates devoid of proteins. LC-MS-based metabolomic (principal component and univariate) analysis unraveled distinct changes in several metabolite levels upon amyloid (but not monomer) incubation. Of 63 metabolites identified, the amounts of four increased (3-hydroxycapric acid, 2-pyrocatechuic acid, adenosine, and NAD), and the amounts of seventeen decreased (including aromatic and apolar amino acids, metabolites in the TCA cycle, keto acids) in the presence of α-synuclein amyloids. Many of these metabolite changes match what has been reported previously in Parkinson's disease patients and animal-model metabolomics studies. Chemical reactivity of α-synuclein amyloids may be a new gain-of-function that alters the metabolite composition in cells and, thereby, modulates disease progression.
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Registered trials
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