ArticleScientific reports2015
Doxycycline hinders phenylalanine fibril assemblies revealing a potential novel therapeutic approach in phenylketonuria.
Article in Scientific reports, 2015. 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, 46 citations in OpenAlex.
- Oh my gut! Is the microbial origin of neurodegenerative diseases real?Infection and immunity · 2023Review
- Chemical Chaperones Modulate the Formation of Metabolite Assemblies.International journal of molecular sciences · 2021Article
- Glucosylceramide Associated with Gaucher Disease Forms Amyloid-like Twisted Ribbon Fibrils That Induce α-Synuclein Aggregation.ACS nano · 2021Article
- Half a century of amyloids: past, present and future.Chemical Society reviews · 2020Review
- Self-Assembly of Aromatic Amino Acid Enantiomers into Supramolecular Materials of High Rigidity.ACS nano · 2020Article
- Ultrashort Peptide Self-Assembly: Front-Runners to Transport Drug and Gene Cargos.Frontiers in bioengineering and biotechnology · 2020Review
- Article
- Fibril formation and therapeutic targeting of amyloid-like structures in a yeast model of adenine accumulation.Nature communications · 2019Article
- Article
- Seeding of proteins into amyloid structures by metabolite assemblies may clarify certain unexplained epidemiological associations.Open biology · 2018Review
- Pediatric use of tetracyclines: focus on neurodevelopmental effects.Pediatric research · 2017Article
- Metabolite amyloids: a new paradigm for inborn error of metabolism disorders.Journal of inherited metabolic disease · 2016Article
Corrections and comments
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Authors and funding
13 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A new paradigm for the aetiopathology of phenylketonuria suggests the presence of amyloid-like assemblies in the brains of transgenic mouse models and patients with phenylketonuria, possibly shedding light on the selective cognitive deficit associated with this disease. Paralleling the amyloidogenic route that identifies different stages of peptide aggregation, corresponding to different levels of toxicity, we experimentally address for the first time, the physico-chemical properties of phenylalanine aggregates via Small Angle, Wide Angle X-ray Scattering and Atomic Force Microscopy. Results are consistent with the presence of well-structured, aligned fibres generated by milliMolar concentrations of phenylalanine. Moreover, the amyloid-modulating doxycycline agent affects the local structure of phenylalanine aggregates, preventing the formation of well-ordered crystalline structures. Phenylalanine assemblies prove toxic in vitro to immortalized cell lines and primary neuronal cells. Furthermore, these assemblies also cause dendritic sprouting alterations and synaptic protein impairment in neurons. Doxycycline counteracts these toxic effects, suggesting an approach for the development of future innovative non-dietary preventive therapies.
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