ArticleJournal of the American Chemical Society2012
Bifunctional compounds for controlling metal-mediated aggregation of the aβ42 peptide.
Article in Journal of the American Chemical Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.
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Who cites it
75 citing papers in PubMed, 199 citations in OpenAlex.
- Pyridinophane Ligands: An Attractive Chelator Platform for Mn-Based Imaging Agents.Journal of medicinal chemistry · 2026Article
- Dexter Energy Transfer Photocatalytic Microdissection of Amyloid Plaques in Alzheimer's Disease.JACS Au · 2026Article
- Highly Efficient and Eco-friendly Synthesis and Bio-activities of 1,3-benzazoles as Cu (II) Chelators in Alzheimer's Disease Therapy.Current medicinal chemistry · 2026Article
- Tolcapone Interferes With Key Pathological Features in Alzheimer's Disease.Bioinorganic chemistry and applications · 2026Article
- Unveiling the Light Induced Energy Transfer Events in Water Soluble Benzothiazole Appended Borondipyrromethene: Synthesis, Photophysical Study, and Applications to Amyloid Binding.Chemistry, an Asian journal · 2026Article
- Donepezil and Memantine Derivatives for Dual-Function and Prodrug Applications in Alzheimer's Disease.ACS chemical neuroscience · 2025Article
- Evaluation of Anti-Alzheimer's Potential of Azo-Stilbene-Thioflavin-T derived Multifunctional Molecules: Synthesis, Metal and Aβ Species Binding and Cholinesterase Activity.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Bifunctional Copper Chelators Capable of Reducing Aβ Aggregation and Aβ-Induced Oxidative Stress.ACS omega · 2024Article
- 2-Phenylbenzothiazolyl iridium complexes as inhibitors and probes of amyloid β aggregation.Dalton transactions (Cambridge, England : 2003) · 2024Article
- Targeting Biometals in Alzheimer's Disease with Metal Chelating Agents Including Coumarin Derivatives.CNS drugs · 2024Review
- Design, synthesis, and evaluation of 2,2'-bipyridyl derivatives as bifunctional agents against Alzheimer's disease.Molecular diversity · 2024Article
- Molecular Insights into Cu/Zn Metal Response to the Amyloid β-Peptide (1-42).ACS physical chemistry Au · 2024Article
- Pleiotropic Potential ofMolecules (Basel, Switzerland) · 2023Article
- Recent progress of small-molecule-based theranostic agents in Alzheimer's disease.RSC medicinal chemistry · 2023Review
- Metal Binding of Alzheimer's Amyloid-β and Its Effect on Peptide Self-Assembly.Accounts of chemical research · 2023Article
- In Situ Raman Study of Neurodegenerated Human Neuroblastoma Cells Exposed to Outer-Membrane Vesicles Isolated fromInternational journal of molecular sciences · 2023Article
- An Electrochemistry and Computational Study at an Electrified Liquid-Liquid Interface for Studying Beta-Amyloid Aggregation.Membranes · 2023Article
- Aβ-Targeting Bifunctional Chelators (BFCs) for Potential Therapeutic and PET Imaging Applications.International journal of molecular sciences · 2022Review
- Spin state dependent peroxidase activity of heme bound amyloid β peptides relevant to Alzheimer's disease.Chemical science · 2022Article
- Article
15 more citing papers are in PubMed but not listed here.
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Abnormal interactions of Cu and Zn ions with the amyloid β (Aβ) peptide are proposed to play an important role in the pathogenesis of Alzheimer's disease (AD). Disruption of these metal-peptide interactions using chemical agents holds considerable promise as a therapeutic strategy to combat this incurable disease. Reported herein are two bifunctional compounds (BFCs) L1 and L2 that contain both amyloid-binding and metal-chelating molecular motifs. Both L1 and L2 exhibit high stability constants for Cu(2+) and Zn(2+) and thus are good chelators for these metal ions. In addition, L1 and L2 show strong affinity toward Aβ species. Both compounds are efficient inhibitors of the metal-mediated aggregation of the Aβ(42) peptide and promote disaggregation of amyloid fibrils, as observed by ThT fluorescence, native gel electrophoresis/Western blotting, and transmission electron microscopy (TEM). Interestingly, the formation of soluble Aβ(42) oligomers in the presence of metal ions and BFCs leads to an increased cellular toxicity. These results suggest that for the Aβ(42) peptide-in contrast to the Aβ(40) peptide-the previously employed strategy of inhibiting Aβ aggregation and promoting amyloid fibril dissagregation may not be optimal for the development of potential AD therapeutics, due to formation of neurotoxic soluble Aβ(42) oligomers.
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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.