ArticleThe Journal of biological chemistry2013
Structural insights into Aβ42 oligomers using site-directed spin labeling.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed.
- Misfolded protein oligomers: mechanisms of formation, cytotoxic effects, and pharmacological approaches against protein misfolding diseases.Molecular neurodegeneration · 2024Review
- EPR Studies of Aβ42 Oligomers Indicate a Parallel In-Register β-Sheet Structure.ACS chemical neuroscience · 2024Article
- Amyloid Precursor Protein and Alzheimer's Disease.International journal of molecular sciences · 2023Review
- Residue-specific binding of Ni(II) ions influences the structure and aggregation of amyloid beta (Aβ) peptides.Scientific reports · 2023Article
- The amyloid concentric β-barrel hypothesis: Models of amyloid beta 42 oligomers and annular protofibrils.Proteins · 2022Article
- Evidence for a Strong Relationship between the Cytotoxicity and Intracellular Location of β-Amyloid.Life (Basel, Switzerland) · 2022Article
- Molecular dynamics study of water channels in natural and synthetic amyloid-β fibrils.The Journal of chemical physics · 2021Article
- Lipid membranes induce structural conversion from amyloid oligomers to fibrils.Biochemical and biophysical research communications · 2021Article
- Segmental structural dynamics in Aβ42 globulomers.Biochemical and biophysical research communications · 2021Article
- Effect of spin labelling on the aggregation kinetics of yeast prion protein Ure2.Royal Society open science · 2021Article
- Characterization of Homogeneous and Heterogeneous Amyloid-β42 Oligomer Preparations with Biochemical Methods and Infrared Spectroscopy Reveals a Correlation between Infrared Spectrum and Oligomer Size.ACS chemical neuroscience · 2021Article
- Alzheimer's Aβ42 and Aβ40 form mixed oligomers with direct molecular interactions.Biochemical and biophysical research communications · 2021Article
- Distinguishing the Effect on the Rate and Yield of Aβ42 Aggregation by Green Tea Polyphenol EGCG.ACS omega · 2020Article
- High-Speed Atomic Force Microscopy Reveals the Structural Dynamics of the Amyloid-β and Amylin Aggregation Pathways.International journal of molecular sciences · 2020Review
- High-resolution probing of early events in amyloid-β aggregation related to Alzheimer's disease.Chemical communications (Cambridge, England) · 2020Review
- Aβ42 fibril formation from predominantly oligomeric samples suggests a link between oligomer heterogeneity and fibril polymorphism.Royal Society open science · 2019Article
- Interference with Amyloid-β Nucleation by Transient Ligand Interaction.Molecules (Basel, Switzerland) · 2019Article
- Key Residues for the Formation of Aβ42 Amyloid Fibrils.ACS omega · 2018Article
- Site-specific structural order in Alzheimer's Aβ42 fibrils.Royal Society open science · 2018Article
- Controlling the Oligomerization State of Aβ-Derived Peptides with Light.Journal of the American Chemical Society · 2018Article
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Oligomerization of the 42-residue peptide Aβ42 plays a key role in the pathogenesis of Alzheimer disease. Despite great academic and medical interest, the structures of these oligomers have not been well characterized. Site-directed spin labeling combined with electron paramagnetic resonance spectroscopy is a powerful approach for studying structurally ill-defined systems, but its application in amyloid oligomer structure study has not been systematically explored. Here we report a comprehensive structural study on a toxic Aβ42 oligomer, called globulomer, using site-directed spin labeling complemented by other techniques. Transmission electron microscopy shows that these oligomers are globular structures with diameters of ∼7-8 nm. Circular dichroism shows primarily β-structures. X-ray powder diffraction suggests a highly ordered intrasheet hydrogen-bonding network and a heterogeneous intersheet packing. Residue-level mobility analysis on spin labels introduced at 14 different positions shows a structured state and a disordered state at all labeling sites. Side chain mobility analysis suggests that structural order increases from N- to C-terminal regions. Intermolecular distance measurements at 14 residue positions suggest that C-terminal residues Gly-29-Val-40 form a tightly packed core with intermolecular distances in a narrow range of 11.5-12.5 Å. These intermolecular distances rule out the existence of fibril-like parallel in-register β-structures and strongly suggest an antiparallel β-sheet arrangement in Aβ42 globulomers.
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