ArticleScientific reports2017
Evidence for Intramolecular Antiparallel Beta-Sheet Structure in Alpha-Synuclein Fibrils from a Combination of Two-Dimensional Infrared Spectroscopy and Atomic Force Microscopy.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.
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Who cites it
72 citing papers in PubMed.
- Multidimensional Infrared Spectroscopy as a Bioanalytical Technique.Chemical reviews · 2026Review
- Nanopipettes Enable Native Mass Spectrometry Studies of the Intrinsically Disordered Protein α-Synuclein in Biochemical Buffers.Analytical chemistry · 2026Article
- Article
- Differences in α-synuclein conformational states in physiologically relevant pH/NaThe Analyst · 2026Article
- Hidden faces of alpha-synuclein: Cryo-EM revelation of fibril polymorphs driven by disease, mutations, and PTMs.BBA advances · 2026Review
- Machine learning analysis of population-wide plasma proteins identifies hormonal biomarkers of Parkinson's disease.Frontiers in aging neuroscience · 2026Article
- Rare Earth Element-Induced Condensation of the Block V of the Repeats-in-Toxin Domain from CyaA fromLangmuir : the ACS journal of surfaces and colloids · 2025Article
- An Optimized Protocol for High-Quality AFM Imaging of Amyloid Fibrils.Bio-protocol · 2025Article
- Amyloid-Like Self-Assembling of Black Soldier Fly Proteins and Development of Bioplastics.ACS sustainable chemistry & engineering · 2025Article
- Navigation Between Alzheimer's Disease (AD) and Its Various Pathophysiological Trajectories: The Pathogenic Link to Neuroimmunology-Genetics and Neuroinflammation.International journal of molecular sciences · 2025Review
- Effect of RNA on the supramolecular architecture of α-synuclein fibrils.Biophysical journal · 2025Article
- Local Ionic Conditions Modulate the Aggregation Propensity and Influence the Structural Polymorphism of α-Synuclein.Journal of the American Chemical Society · 2025Article
- Article
- High-Yield α-Synuclein Purification and Ionic Strength Modification Pivotal to Seed Amplification Assay Performance and Reproducibility.International journal of molecular sciences · 2024Article
- Dynamical Transition in Dehydrated Proteins.The journal of physical chemistry letters · 2024Article
- Liquid-liquid phase separation and conformational strains ofFrontiers in molecular neuroscience · 2024Review
- α-Synuclein emulsifies TDP-43 prion-like domain-RNA liquid droplets to promote heterotypic amyloid fibrils.Communications biology · 2023Article
- RNA sequestration driven by amyloid formation: the alpha synuclein case.Nucleic acids research · 2023Article
- Sulfated Polysaccharides as a Fighter with Protein Non-Physiological Aggregation: The Role of Polysaccharide Flexibility and Charge Density.International journal of molecular sciences · 2023Article
- Unpolarized laser method for infrared spectrum calculation of amide I CO bonds in proteins using molecular dynamics simulation.Computers in biology and medicine · 2023Article
12 more citing papers are in PubMed but not listed here.
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6 authors.
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No grant is acknowledged in the PubMed record.
Abstract
The aggregation of the intrinsically disordered protein alpha-synuclein (αS) into amyloid fibrils is thought to play a central role in the pathology of Parkinson's disease. Using a combination of techniques (AFM, UV-CD, XRD, and amide-I 1D- and 2D-IR spectroscopy) we show that the structure of αS fibrils varies as a function of ionic strength: fibrils aggregated in low ionic-strength buffers ([NaCl] ≤ 25 mM) have a significantly different structure than fibrils grown in higher ionic-strength buffers. The observations for fibrils aggregated in low-salt buffers are consistent with an extended conformation of αS molecules, forming hydrogen-bonded intermolecular β-sheets that are loosely packed in a parallel fashion. For fibrils aggregated in high-salt buffers (including those prepared in buffers with a physiological salt concentration) the measurements are consistent with αS molecules in a more tightly-packed, antiparallel intramolecular conformation, and suggest a structure characterized by two twisting stacks of approximately five hydrogen-bonded intermolecular β-sheets each. We find evidence that the high-frequency peak in the amide-I spectrum of αS fibrils involves a normal mode that differs fundamentally from the canonical high-frequency antiparallel β-sheet mode. The high sensitivity of the fibril structure to the ionic strength might form the basis of differences in αS-related pathologies.
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