ArticleInternational journal of molecular sciences2018
Unveiling a Selective Mechanism for the Inhibition of α-Synuclein Aggregation by β-Synuclein.
Article in International journal of molecular sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 26 citations in OpenAlex.
- Divalent and Trivalent Metallic Ions Differentially Affect Alpha-Synuclein Aggregation.ACS chemical neuroscience · 2025Article
- Comparative Analysis of Aggregation of β- and γ-Synucleins in Vertebrates.Biomolecules · 2025Article
- Positron emission tomography tracers for synucleinopathies.Molecular neurodegeneration · 2025Review
- β-synuclein regulates the phase transitions and amyloid conversion of α-synuclein.Nature communications · 2024Article
- α-Synuclein Strains and Their Relevance to Parkinson's Disease, Multiple System Atrophy, and Dementia with Lewy Bodies.International journal of molecular sciences · 2023Review
- Article
- The Synucleins and the Astrocyte.Biology · 2023Review
- Age-Related Changes of the Synucleins Profile in the Mouse Retina.Biomolecules · 2023Article
- β-Synuclein: An Enigmatic Protein with Diverse Functionality.Biomolecules · 2022Review
- Excess membrane binding of monomeric alpha-, beta- and gamma-synuclein is invariably associated with inclusion formation and toxicity.Human molecular genetics · 2021Article
- Selectivity of Lewy body protein interactions along the aggregation pathway of α-synuclein.Communications biology · 2021Article
- Increased Dynamics of α-Synuclein Fibrils by β-Synuclein Leads to Reduced Seeding and Cytotoxicity.Scientific reports · 2019Article
- Novel Mannitol-Based Small Molecules for Inhibiting Aggregation of α-Synuclein Amyloids in Parkinson's Disease.Frontiers in molecular biosciences · 2019Article
- Pathological mutations differentially affect the self-assembly and polymerisation of the innate immune system signalling adaptor molecule MyD88.BMC biology · 2018Article
- Interactions between the Intrinsically Disordered Proteins β-Synuclein and α-Synuclein.Proteomics · 2018Review
- Multi-Pronged Interactions Underlie Inhibition of α-Synuclein Aggregation by β-Synuclein.Journal of molecular biology · 2018Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
α-Synuclein (αS) is an intrinsically disordered protein that is associated with Parkinson's disease (PD) through its ability to self-assemble into oligomers and fibrils. Inhibition of this oligomerization cascade is an interesting approach to developing therapeutical strategies and β-synuclein (βS) has been described as a natural negative regulator of this process. However, the biological background and molecular mechanisms by which this inhibition occurs is unclear. Herein, we focused on assessing the effect of βS on the aggregation of five αS pathological mutants linked to early-onset PD (A30P, E46K, H50Q, G51D and A53T). By coupling single molecule fluorescence spectroscopy to a cell-free protein expression system, we validated the ability of βS to act as a chaperone of αS, effectively inhibiting its aggregation. Interestingly, we found that βS does so in a selective manner, i.e., is a more effective inhibitor for certain αS pathological mutants-A30P and G51D-as compared to E46K, H50Q and A53T. Moreover, two-color coincidence experiments proved that this discrepancy is due to a preferential incorporation of βS into smaller oligomers of αS. This was validated by showing that the chaperoning effect was lost when proteins were mixed after being expressed individually. This study highlights the potential of fluorescence spectroscopy to deconstruct αS aggregation cascade and its interplay with βS.
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