ArticleACS chemical neuroscience2013
On-surface aggregation of α-synuclein at nanomolar concentrations results in two distinct growth mechanisms.
Article in ACS chemical neuroscience, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 76 citations in OpenAlex.
- α-Synuclein aggregation landscape from phase separation to neurotoxic intermediates.FEBS letters · 2026Review
- Membrane interfacial potential governs surface condensation and fibrillation of α-Synuclein in neurons.Nature communications · 2026Article
- A mechanistic model of pure and lipidic α-synuclein aggregation for advancing Parkinson's therapies.Communications chemistry · 2025Article
- The Role of α-Synuclein-DNAJB6b Coaggregation in Amyloid Suppression.ACS chemical neuroscience · 2025Article
- MJF-14 proximity ligation assay detects early non-inclusion alpha-synuclein pathology with enhanced specificity and sensitivity.NPJ Parkinson's disease · 2024Article
- FUS fibrillation occurs through a nucleation-based process below the critical concentration required for liquid-liquid phase separation.Scientific reports · 2023Article
- A proteome scale study reveals how plastic surfaces and agitation promote protein aggregation.Scientific reports · 2023Article
- Stability matters, too - the thermodynamics of amyloid fibril formation.Chemical science · 2022Review
- Near-Wall Aggregation of Amyloidogenic Aβ 1-40 Peptide: Direct Observation by the FRET.Molecules (Basel, Switzerland) · 2021Article
- Amyloids as Building Blocks for Macroscopic Functional Materials: Designs, Applications and Challenges.International journal of molecular sciences · 2021Review
- Nanoscale Surface Topography Modulates hIAPP Aggregation Pathways at Solid-Liquid Interfaces.International journal of molecular sciences · 2021Article
- Effect of Surface Roughness on Aggregation of Polypeptide Chains: A Monte Carlo Study.Biomolecules · 2021Article
- Biophysical processes underlying cross-seeding in amyloid aggregation and implications in amyloid pathology.Biophysical chemistry · 2021Review
- Alpha-Synuclein-Nanoparticle Interactions: Understanding, Controlling and Exploiting Conformational Plasticity.Molecules (Basel, Switzerland) · 2020Review
- Article
- Membranes as modulators of amyloid protein misfolding and target of toxicity.Biochimica et biophysica acta. Biomembranes · 2018Review
- Structural insights from lipid-bilayer nanodiscs link α-Synuclein membrane-binding modes to amyloid fibril formation.Communications biology · 2018Article
- Nanoscale Dynamics of Amyloid β-42 Oligomers As Revealed by High-Speed Atomic Force Microscopy.ACS nano · 2017Article
- Factors affecting the physical stability (aggregation) of peptide therapeutics.Interface focus · 2017Review
- Supercritical angle Raman microscopy: a surface-sensitive nanoscale technique without field enhancement.Light, science & applications · 2017Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The aggregation of α-synuclein (α-Syn) is believed to be one of the key steps driving the pathology of Parkinson's disease and related neurodegenerative disorders. One of the present hypotheses is that the onset of such pathologies is related to the rise of α-Syn levels above a critical concentration at which toxic oligomers or mature fibrils are formed. In the present study, we find that α-Syn aggregation in vitro is a spontaneous process arising at bulk concentrations as low as 1 nM and below in the presence of both hydrophilic glass surfaces and cell membrane mimicking supported lipid bilayers (SLBs). Using three-dimensional supercritical angle fluorescence (3D-SAF) microscopy, we observed the process of α-Syn aggregation in situ. As soon as α-Syn monomers were exposed to the surface, they started to adsorb and aggregate along the surface plane without a prior lag phase. However, at a later stage of the aggregation process, a second type of aggregate was observed. In contrast to the first type, these aggregates showed an extended structure being tethered with one end to the surface and being mobile at the other end, which protruded into the solution. While both types of α-Syn aggregates were found to contain amyloid structures, their growing mechanisms turned out to be significantly different. Given the clear evidence that surface-induced α-Syn aggregation in vitro can be triggered at bulk concentrations far below physiological concentrations, the concept of a critical concentration initiating aggregation in vivo needs to be reconsidered.
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