ArticleBiophysical journal2021
Macromolecular crowding modulates α-synuclein amyloid fiber growth.
Article in Biophysical journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 53 citations in OpenAlex.
- The endoplasmic reticulum displays high polarity with low protein aggregation in human cells.Communications biology · 2026Article
- A global thermodynamic-kinetic model capturing the hallmarks of liquid-liquid phase separation and amyloid aggregation.Cell reports. Physical science · 2026Article
- Surface-modified protein crowders influence mutant huntingtin exon 1 aggregation via crowding effects, crowder association, and crowder solution stability.Protein science : a publication of the Protein Society · 2025Article
- Alpha-synuclein fibril structures cluster into distinct classes.Biophysical journal · 2025Review
- Underestimated role of macromolecular crowding in bioengineeredMaterials today. Bio · 2025Article
- Secondary nucleation as a strategy towards hierarchically organized mesoscale topologies in supramolecular polymerization.Nature chemistry · 2025Review
- Phase Separation and Aggregation of α-Synuclein Diverge at Different Salt Conditions.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- α-Synuclein oligomers form by secondary nucleation.Nature communications · 2024Article
- Article
- Molecular Crowding: The History and Development of a Scientific Paradigm.Chemical reviews · 2024Review
- Phase Separation and Aggregation of α-Synuclein Diverge at Different Salt Conditions.bioRxiv : the preprint server for biology · 2024Article
- The effects of biological crowders on fibrillization, structure, diffusion, and conformational dynamics of α-synuclein.Protein science : a publication of the Protein Society · 2024Article
- Distinct growth regimes of α-synuclein amyloid elongation.Biophysical journal · 2023Article
- Macromolecular Crowding Is Surprisingly Unable to Deform the Structure of a Model Biomolecular Condensate.Biology · 2023Article
- Crowding-induced phase separation and gelling by co-condensation of PEG in NPM1-rRNA condensates.Biophysical journal · 2023Article
- Secondary Structure in Amyloids in Relation to Their Wild Type Forms.International journal of molecular sciences · 2022Article
- Crossroads between copper ions and amyloid formation in Parkinson's disease.Essays in biochemistry · 2022Article
- Molecular Mechanisms of Inhibition of Protein Amyloid Fibril Formation: Evidence and Perspectives Based on Kinetic Models.International journal of molecular sciences · 2022Review
- Protein folding in vitro and in the cell: From a solitary journey to a team effort.Biophysical chemistry · 2022Review
- Atomistic Simulation of Lysozyme in Solutions Crowded by Tetraethylene Glycol: Force Field Dependence.Molecules (Basel, Switzerland) · 2022Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The crowdedness of living cells, hundreds of milligrams per milliliter of macromolecules, may affect protein folding, function, and misfolding. Still, such processes are most often studied in dilute solutions in vitro. To assess consequences of the in vivo milieu, we here investigated the effects of macromolecular crowding on the amyloid fiber formation reaction of α-synuclein, the amyloidogenic protein in Parkinson's disease. For this, we performed spectroscopic experiments probing individual steps of the reaction as a function of the macromolecular crowding agent Ficoll70, which is an inert sucrose-based polymer that provides excluded-volume effects. The experiments were performed at neutral pH at quiescent conditions to avoid artifacts due to shaking and glass beads (typical conditions for α-synuclein), using amyloid fiber seeds to initiate reactions. We find that both primary nucleation and fiber elongation steps during α-synuclein amyloid formation are accelerated by the presence of 140 and 280 mg/mL Ficoll70. Moreover, in the presence of Ficoll70 at neutral pH, secondary nucleation appears favored, resulting in faster overall α-synuclein amyloid formation. In contrast, sucrose, a small-molecule osmolyte and building block of Ficoll70, slowed down α-synuclein amyloid formation. The ability of cell environments to modulate reaction kinetics to a large extent, such as severalfold faster individual steps in α-synuclein amyloid formation, is an important consideration for biochemical reactions in living systems.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.