ArticleThe Journal of biological chemistry2012
Small amphipathic molecules modulate secondary structure and amyloid fibril-forming kinetics of Alzheimer disease peptide Aβ(1-42).
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 46 citations in OpenAlex.
- Amodiaquine Modulates Aggregation and Disassembly of Amyloid-β and Tau and Attenuates Neuroinflammatory Responses and Aβ Production.Pharmaceutics · 2025Article
- Age- and Sex-Specific Regulation of Serine Racemase in the Retina of an Alzheimer's Disease Mouse.Investigative ophthalmology & visual science · 2025Article
- Article
- Early onset diagnosis in Alzheimer's disease patients via amyloid-β oligomers-sensing probe in cerebrospinal fluid.Nature communications · 2024Article
- Nanotechnology for microglial targeting and inhibition of neuroinflammation underlying Alzheimer's pathology.Translational neurodegeneration · 2024Article
- Free Gangliosides Can Alter Amyloid-β Aggregation.The journal of physical chemistry letters · 2022Article
- The intriguing dose-dependent effect of selected amphiphilic compounds on insulin amyloid aggregation: Focus on a cholesterol-based detergent, Chobimalt.Frontiers in molecular biosciences · 2022Article
- Retinal hyperspectral imaging in the 5xFAD mouse model of Alzheimer's disease.Scientific reports · 2021Article
- Biflavonoid-Induced Disruption of Hydrogen Bonds Leads to Amyloid-β Disaggregation.International journal of molecular sciences · 2021Article
- The Amphipathic GM1 Molecule Stabilizes Amyloid Aggregates, Preventing their Cytotoxicity.Biophysical journal · 2020Article
- Polyphenolic Biflavonoids Inhibit Amyloid-Beta Fibrillation and Disaggregate Preformed Amyloid-Beta Fibrils.Biomolecules & therapeutics · 2020Article
- A Novel pH-Tunable Secondary Conformation Containing Mixed Micellar System in Anticancer Treatment.Cancers · 2020Article
- Protein folding, misfolding and aggregation: The importance of two-electron stabilizing interactions.PloS one · 2017Article
- Apolipoprotein C-II Adopts Distinct Structures in Complex with Micellar and Submicellar Forms of the Amyloid-Inhibiting Lipid-Mimetic Dodecylphosphocholine.Biophysical journal · 2016Article
- Controllable Phase Separation by Boc-Modified Lipophilic Acid as a Multifunctional Extractant.Scientific reports · 2015Article
- Chemical Fluorescent Probe for Detection of Aβ Oligomers.Journal of the American Chemical Society · 2015Article
- Anti-amyloidogenic properties of some phenolic compounds.Biomolecules · 2015Article
- Stabilization of nontoxic Aβ-oligomers: insights into the mechanism of action of hydroxyquinolines in Alzheimer's disease.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015Article
- Article
- Molecular interactions of Alzheimer's biomarker FDDNP with Aβ peptide.Biophysical journal · 2012Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amyloid fibril formation is associated with a number of debilitating systemic and neurodegenerative diseases. One of the most prominent is Alzheimer disease in which aggregation and deposition of the Aβ peptide occur. Aβ is widely considered to mediate the extensive neuronal loss observed in this disease through the formation of soluble oligomeric species, with the final fibrillar end product of the aggregation process being relatively inert. Factors that influence the aggregation of these amyloid-forming proteins are therefore very important. We have screened a library of 96 amphipathic molecules for effects on Aβ(1-42) aggregation and self-association. We find, using thioflavin T fluorescence and electron microscopy assays, that 30 of the molecules inhibit the aggregation process, whereas 36 activate fibril formation. Several activators and inhibitors were subjected to further analysis using analytical ultracentrifugation and circular dichroism. Activators typically display a 1:10 peptide:detergent stoichiometry for maximal activation, whereas the inhibitors are effective at a 1:1 stoichiometry. Analytical ultracentrifugation and circular dichroism experiments show that activators promote a mixture of unfolded and β-sheet structures and rapidly form large aggregates, whereas inhibitors induce α-helical structures that form stable dimeric/trimeric oligomers. The results suggest that Aβ(1-42) contains at least one small molecule binding site, which modulates the secondary structure and aggregation processes. Further studies of the binding of these compounds to Aβ may provide insight for developing therapeutic strategies aimed at stabilizing Aβ in a favorable conformation.
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