ArticlePeerJ2013
Ammonium hydroxide treatment of Aβ produces an aggregate free solution suitable for biophysical and cell culture characterization.
Article in PeerJ, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
55 citing papers in PubMed, 122 citations in OpenAlex.
- Deregulation of Synaptic Plasticity-Related MicroRNAs After Repetitive Transcranial Magnetic Stimulation in Alzheimer's Disease.Molecular neurobiology · 2026Trial
- SEC Purified Monomeric Aβ42 Produces Reproducible and Reliable Aggregation Measurements.bioRxiv : the preprint server for biology · 2026Article
- Bacterial polar metabolites modulate β-amyloid toxicity and cholinergic dysfunction in models of Alzheimer's disease.Scientific reports · 2026Article
- Bidirectional relationship between the biofilm ofMicrobiology spectrum · 2026Article
- The microtubule nexus linking amyloid beta and tau: A simple and unifying theory for the underlying cause of Alzheimer's disease.PNAS nexus · 2026Article
- Amodiaquine Modulates Aggregation and Disassembly of Amyloid-β and Tau and Attenuates Neuroinflammatory Responses and Aβ Production.Pharmaceutics · 2025Article
- Endogenous Aβ and Exogenous Wheat Gluten Nanostructures: Understanding Peptide Self-Assembly in Disease.ACS nano · 2025Review
- Structure-based discovery of forsythoside A as an effective inhibitor to reduce the neurotoxicity of amyloid β.Communications chemistry · 2025Article
- Lysophosphatidylcholine promoting α-Synuclein aggregation in Parkinson's disease: disrupting GCase glycosylation and lysosomal α-Synuclein degradation.NPJ Parkinson's disease · 2025Article
- Different amyloid β42 preparations induce different cell death pathways in the model of SH-SY5Y neuroblastoma cells.Cellular & molecular biology letters · 2024Article
- Brazilian kefir fraction mitigates the Alzheimer-like phenotype in Drosophila melanogaster with β-amyloid overexpression model.Scientific reports · 2024Article
- Enhanced phagocytosis associated with multinucleated microglia via Pyk2 inhibition in an acute β-amyloid infusion model.Journal of neuroinflammation · 2024Article
- Human cystatin C induces the disaggregation process of selected amyloid beta peptides: a structural and kinetic view.Scientific reports · 2023Article
- Mitochondrial DNA variation in Alzheimer's disease reveals a unique microprotein called SHMOOSE.Molecular psychiatry · 2023Article
- Molecularly imprinted sensor based on poly-o-phenylenediamine-hydroquinone polymer for β-amyloid-42 detection.Analytical and bioanalytical chemistry · 2023Article
- Aβ42 oligomer-specific antibody ALZ-201 reduces the neurotoxicity of Alzheimer's disease brain extracts.Alzheimer's research & therapy · 2022Article
- Protofibrillar Amyloid Beta Modulation of Recombinant hCaV2.2 (N-Type) Voltage-Gated Channels.Pharmaceuticals (Basel, Switzerland) · 2022Article
- Fluorescent aptasensor based on conformational switch-induced hybridization for facile detection of β-amyloid oligomers.Analytical and bioanalytical chemistry · 2022Article
- Review
- A robust preparation method for the amyloidogenic and intrinsically disordered amyloid-α peptide.Journal of peptide science : an official publication of the European Peptide Society · 2022Article
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Alzheimer's disease is the leading cause of dementia in the elderly. Pathologically it is characterized by the presence of amyloid plaques and neuronal loss within the brain tissue of affected individuals. It is now widely hypothesised that fibrillar structures represent an inert structure. Biophysical and toxicity assays attempting to characterize the formation of both the fibrillar and the intermediate oligomeric structures of Aβ typically involves preparing samples which are largely monomeric; the most common method by which this is achieved is to use the fluorinated organic solvent 1,1,1,3,3,3-hexafluoro-2-propanol (HFIP). Recent evidence has suggested that this method is not 100% effective in producing an aggregate free solution. We show, using dynamic light scattering, size exclusion chromatography and small angle X-ray scattering that this is indeed the case, with HFIP pretreated Aβ peptide solutions displaying an increased proportion of oligomeric and aggregated material and an increased propensity to aggregate. Furthermore we show that an alternative technique, involving treatment with strong alkali results in a much more homogenous solution that is largely monomeric. These techniques for solubilising and controlling the oligomeric state of Aβ are valuable starting points for future biophysical and toxicity assays.
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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.