ArticleProceedings of the National Academy of Sciences of the United States of America2018
Identification and nanomechanical characterization of the fundamental single-strand protofilaments of amyloid α-synuclein fibrils.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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Who cites it
58 citing papers in PubMed.
- Redesign of TALE proteins for DNA-templated assembly of protein fibers.Nature communications · 2026Article
- Changes in the concentration of phosphatidylcholine in lipid bilayers determines the aggregation rate of transthyretin.Biophysical chemistry · 2026Article
- Nanoscale Analysis beyond Imaging by Atomic Force Microscopy: Molecular Perspectives on Oncology and Neurodegeneration.Small science · 2025Review
- Recent Advances in Amyloids Structural Studies and Thin Film Applications.Molecules (Basel, Switzerland) · 2025Review
- Effect of RNA on the supramolecular architecture of α-synuclein fibrils.Biophysical journal · 2025Article
- The role of phospholipid saturation and composition in α-synuclein aggregation and toxicity: A dual in vitro and in vivo approach.Protein science : a publication of the Protein Society · 2025Article
- Nanotechnology meets medicine: applications of atomic force microscopy in disease.Biophysical reviews · 2025Review
- Detection of protein oligomers with nanopores.Nature reviews. Chemistry · 2025Review
- Molecular Determinants of Protein Pathogenicity at the Single-Aggregate Level.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Nanoscale Structural Characterization of Amyloid β 1-42 Oligomers and Fibrils Grown in the Presence of Fatty Acids.ACS chemical neuroscience · 2024Article
- Under Heparin-Free Conditions Unsaturated Phospholipids Inhibit the Aggregation of 1N4R and 2N4R Tau.The journal of physical chemistry letters · 2024Article
- Hierarchical Protofilament Intertwining Rules the Formation of Mixed-Curvature Amyloid Polymorphs.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Self-Blinking Thioflavin T for Super-resolution Imaging.The journal of physical chemistry letters · 2024Article
- The influence of zwitterionic and anionic phospholipids on protein aggregation.Biophysical chemistry · 2024Review
- Maturation-dependent changes in the size, structure and seeding capacity of Aβ42 amyloid fibrils.Communications biology · 2024Article
- Phospholipids and Cholesterol Determine Molecular Mechanisms of Cytotoxicity of α-Synuclein Oligomers and Fibrils.ACS chemical neuroscience · 2024Article
- Cholesterol and Sphingomyelin Uniquely Alter the Rate of Transthyretin Aggregation and Decrease the Toxicity of Amyloid Fibrils.The journal of physical chemistry letters · 2023Article
- Nanoscale structural characterization of transthyretin aggregates formed at different time points of protein aggregation using atomic force microscopy-infrared spectroscopy.Protein science : a publication of the Protein Society · 2023Article
- Multiplexed Digital Characterization of Misfolded Protein Oligomers via Solid-State Nanopores.Journal of the American Chemical Society · 2023Article
- Saturation of fatty acids in phosphatidic acid uniquely alters transthyretin stability changing morphology and toxicity of amyloid fibrils.Chemistry and physics of lipids · 2023Article
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Authors and funding
6 authors.
Funding
Abstract
The formation and spreading of amyloid aggregates from the presynaptic protein α-synuclein in the brain play central roles in the pathogenesis of Parkinson's disease. Here, we use high-resolution atomic force microscopy to investigate the early oligomerization events of α-synuclein with single monomer angstrom resolution. We identify, visualize, and characterize directly the smallest elementary unit in the hierarchical assembly of amyloid fibrils, termed here single-strand protofilaments. We show that protofilaments form from the direct molecular assembly of unfolded monomeric α-synuclein polypeptide chains. To unravel protofilaments' internal structure and elastic properties, we manipulated nanomechanically these species by atomic force spectroscopy. The single-molecule scale identification and characterization of the fundamental unit of amyloid assemblies provide insights into early events underlying their formation and shed light on opportunities for therapeutic intervention at the early stages of aberrant protein self-assembly.
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