ArticleScientific reports2017
Intrinsic property of phenylalanine to trigger protein aggregation and hemolysis has a direct relevance to phenylketonuria.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 86 citations in OpenAlex.
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- A Diphenylalanine Based Pentapeptide with Fibrillating Self-Assembling Properties.Pharmaceutics · 2023Article
- Non-Targeted Metabolomics Approach Revealed Significant Changes in Metabolic Pathways in Patients with Chronic Traumatic Encephalopathy.Biomedicines · 2022Article
- Mimosine functionalized gold nanoparticles (Mimo-AuNPs) suppress β-amyloid aggregation and neuronal toxicity.Bioactive materials · 2021Article
- ASL expression in ALDH1A1Human genetics · 2021Article
- Glucosylceramide Associated with Gaucher Disease Forms Amyloid-like Twisted Ribbon Fibrils That Induce α-Synuclein Aggregation.ACS nano · 2021Article
- Homocysteine fibrillar assemblies display cross-talk with Alzheimer's disease β-amyloid polypeptide.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Engineering Organoids forFrontiers in molecular neuroscience · 2021Review
- Biofunctionality of Enzymatically Derived Peptides from Codfish (Marine drugs · 2020Article
- Half a century of amyloids: past, present and future.Chemical Society reviews · 2020Review
- Induction of retinopathy by fibrillar oxalate assemblies.Communications chemistry · 2020Article
- Article
- Seeding of proteins into amyloid structures by metabolite assemblies may clarify certain unexplained epidemiological associations.Open biology · 2018Review
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4 authors at 2 institutions in 1 country.
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Abstract
Excess accumulation of phenylalanine is the characteristic of untreated Phenylketonuria (PKU), a well-known genetic abnormality, which triggers several neurological, physical and developmental severities. However, the fundamental mechanism behind the origin of such diverse health problems, particularly the issue of how they are related to the build-up of phenylalanine molecules in the body, is largely unknown. Here, we show cross-seeding ability of phenylalanine fibrils that can effectively initiate an aggregation process in proteins under physiological conditions, converting native protein structures to β-sheet assembly. The resultant fibrils were found to cause severe hemolysis, yielding a plethora of deformed erythrocytes that is highly relevant to phenylketonuria. Unique arrangement of zwitterionic phenylalanine molecules in their amyloid-like higher order entities is predicted to promote both hydrophobic and electrostatic interaction, sufficient enough to trap proteins and to preferentially interact with the membrane components of RBCs. Since the prevalence of hemolysis and amyloid related psychoneurological severities are mostly observed in PKU patients, we propose that the inherent property of phenylalanine fibrils to trigger hemolysis and to induce protein aggregation may have direct relevance to the disease mechanism of PKU.
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