ArticleBiopolymers2016
Effect of acidic pH on the stability of α-synuclein dimers.
Article in Biopolymers, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Differences in α-synuclein conformational states in physiologically relevant pH/NaThe Analyst · 2026Article
- Expanding our understanding of synucleinopathies: proteinopathy, proteinopenia, and lipidopathy.The FEBS journal · 2025Review
- Alpha synuclein and inflammaging.Heliyon · 2025Review
- pH Effects Can Dominate Chemical Shift Perturbations inACS chemical neuroscience · 2023Article
- The Role of α-Synuclein in the Regulation of Serotonin System: Physiological and Pathological Features.Biomedicines · 2023Review
- SNARE Proteins Mediate α-Synuclein Secretion via Multiple Vesicular Pathways.Molecular neurobiology · 2022Article
- Glucosylceramide Associated with Gaucher Disease Forms Amyloid-like Twisted Ribbon Fibrils That Induce α-Synuclein Aggregation.ACS nano · 2021Article
- Monitoring alpha-synuclein oligomerization and aggregation using bimolecular fluorescence complementation assays: What you see is not always what you get.Journal of neurochemistry · 2021Article
- A pH-eQTL Interaction at theFrontiers in aging neuroscience · 2021Article
- Targeting α-Synuclein in Parkinson's Disease by Induced Pluripotent Stem Cell Models.Frontiers in neurology · 2021Review
- Review
- Spontaneous self-assembly of amyloid β (1-40) into dimers.Nanoscale advances · 2019Article
- Probing the Basis of α-Synuclein Aggregation by Comparing Simulations to Single-Molecule Experiments.Biophysical journal · 2019Article
- Force clamp approach for characterization of nano-assembly in amyloid beta 42 dimer.Nanoscale · 2019Article
- Living in Promiscuity: The Multiple Partners of Alpha-Synuclein at the Synapse in Physiology and Pathology.International journal of molecular sciences · 2019Review
- The Non-amyloidal Component Region of α-Synuclein Is Important for α-Synuclein Transport Within Axons.Frontiers in cellular neuroscience · 2019Article
- Probing Intermolecular Interactions within the Amyloid β Trimer Using a Tethered Polymer Nanoarray.Bioconjugate chemistry · 2018Article
- Single-molecule probing of amyloid nano-ensembles using the polymer nanoarray approach.Physical chemistry chemical physics : PCCP · 2017Article
- Nano-assembly of amyloid β peptide: role of the hairpin fold.Scientific reports · 2017Article
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7 authors.
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Abstract
Environmental factors, such as acidic pH, facilitate the assembly of α-synuclein (α-Syn) in aggregates, but the impact of pH on the very first step of α-Syn aggregation remains elusive. Recently, we developed a single-molecule approach that enabled us to measure directly the stability of α-Syn dimers. Unlabeled α-Syn monomers were immobilized on a substrate, and fluorophore-labeled monomers were added to the solution to allow them to form dimers with immobilized α-Syn monomers. The dimer lifetimes were measured directly from the fluorescence bursts on the time trajectories. Herein, we applied the single-molecule tethered approach for probing of intermolecular interaction to characterize the effect of acidic pH on the lifetimes of α-Syn dimers. The experiments were performed at pH 5 and 7 for wild-type α-Syn and for two mutants containing familial type mutations E46K and A53T. We demonstrate that a decrease of pH resulted in more than threefold increase in the α-Syn dimers lifetimes with some variability between the α-Syn species. We hypothesize that the stabilization effect is explained by neutralization of residues 96-140 of α-Syn and this electrostatic effect facilitates the association of the two monomers. Given that dimerization is the first step of α-Syn aggregation, we posit that the electrostatic effect thereby contributes to accelerating α-Syn aggregation at acidic pH. © 2016 Wiley Periodicals, Inc. Biopolymers 105: 715-724, 2016.
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