ArticleACS chemical neuroscience2021
Characterization of Homogeneous and Heterogeneous Amyloid-β42 Oligomer Preparations with Biochemical Methods and Infrared Spectroscopy Reveals a Correlation between Infrared Spectrum and Oligomer Size.
Article in ACS chemical neuroscience, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 49 citations in OpenAlex.
- Posterior parietal cortex oscillatory activity reflects persistent spatial memory impairments induced by early hippocampal amyloidosis in male mice.The Journal of physiology · 2026Article
- Spectroscopic secondary structure fingerprint of β-variant of SARS-CoV-2 spike glycoprotein.European biophysics journal : EBJ · 2026Article
- Multimodal Structural Characterization of SARS-CoV-2 Spike Variants: Spectroscopic and Computational Insights.International journal of molecular sciences · 2025Article
- Endogenous Aβ and Exogenous Wheat Gluten Nanostructures: Understanding Peptide Self-Assembly in Disease.ACS nano · 2025Review
- Chameleonic Nature of Aβ: Implications for Alzheimer's and Other Amyloid Diseases.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025Review
- Article
- Molecular interactions, structural effects, and binding affinities between silver ions (AgScientific reports · 2025Article
- Fourier Transform Infrared Spectroscopy Analysis as a Tool to Address Aβ Impact on Extracellular Vesicles.Molecules (Basel, Switzerland) · 2025Article
- Fourier transform infrared spectroscopy detects distinct TAR DNA-binding protein 43 signatures in frontotemporal lobar degeneration.Frontiers in neuroscience · 2025Article
- Infrared Spectroscopy of SARS-CoV-2 Viral Protein: from Receptor Binding Domain to Spike Protein.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Characterization of Uranyl (UOACS chemical neuroscience · 2023Article
- Length and saturation of fatty acids in phosphatidylserine determine the rate of lysozyme aggregation simultaneously altering the structure and toxicity of amyloid oligomers and fibrils.Protein science : a publication of the Protein Society · 2023Article
- Lipids uniquely alter the secondary structure and toxicity of amyloid beta 1-42 aggregates.The FEBS journal · 2023Article
- Elucidation of the Effect of Phospholipid Charge on the Rate of Insulin Aggregation and Structure and Toxicity of Amyloid Fibrils.ACS omega · 2023Article
- Nanoscale imaging of individual amyloid aggregates extracted from brains of Alzheimer and Parkinson patients reveals presence of lipids in α-synuclein but not in amyloid βProtein science : a publication of the Protein Society · 2023Article
- Residue-specific binding of Ni(II) ions influences the structure and aggregation of amyloid beta (Aβ) peptides.Scientific reports · 2023Article
- Infrared Diffusion-Ordered Spectroscopy Reveals Molecular Size and Structure.Angewandte Chemie (International ed. in English) · 2023Article
- Lipids uniquely alter rates of insulin aggregation and lower toxicity of amyloid aggregates.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2023Article
- Nanoscale Characterization of Parallel and Antiparallel β-Sheet Amyloid Beta 1-42 Aggregates.ACS chemical neuroscience · 2022Article
- Methodological advances and strategies for high resolution structure determination of cellular protein aggregates.The Journal of biological chemistry · 2022Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Soluble oligomers of the amyloid-β(1-42) (Aβ42) peptide, widely considered to be among the relevant neurotoxic species involved in Alzheimer's disease, were characterized with a combination of biochemical and biophysical methods. Homogeneous and stable Aβ42 oligomers were prepared by treating monomeric solutions of the peptide with detergents. The prepared oligomeric solutions were analyzed with blue native and sodium dodecyl sulfate polyacrylamide gel electrophoresis, as well as with infrared (IR) spectroscopy. The IR spectra indicated a well-defined β-sheet structure of the prepared oligomers. We also found a relationship between the size/molecular weight of the Aβ42 oligomers and their IR spectra: The position of the main amide I' band of the peptide backbone correlated with oligomer size, with larger oligomers being associated with lower wavenumbers. This relationship explained the time-dependent band shift observed in time-resolved IR studies of Aβ42 aggregation in the absence of detergents, during which the oligomer size increased. In addition, the bandwidth of the main IR band in the amide I' region was found to become narrower with time in our time-resolved aggregation experiments, indicating a more homogeneous absorption of the β-sheets of the oligomers after several hours of aggregation. This is predominantly due to the consumption of smaller oligomers in the aggregation process.
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