ArticleInorganic chemistry2014
Small bifunctional chelators that do not disaggregate amyloid β fibrils exhibit reduced cellular toxicity.
Article in Inorganic chemistry, 2014. 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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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
20 citing papers in PubMed, 47 citations in OpenAlex.
- Ligands for Protein Fibrils of Amyloid-β, α-Synuclein, and Tau.Chemical reviews · 2025Review
- 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
- Turn-on fluorescent sensors for Cu-rich amyloid β peptide aggregates.Sensors & diagnostics · 2022Article
- Copper chelating cyclic peptidomimetic inhibits Aβ fibrillogenesis.RSC medicinal chemistry · 2022Article
- Rational Design of a Cu Chelator That Mitigates Cu-Induced ROS Production by Amyloid Beta.Chembiochem : a European journal of chemical biology · 2022Article
- Novel Benzothiazole-Based Highly Selective Ratiometric Fluorescent Turn-On Sensors for ZnACS omega · 2021Article
- Amphiphilic Distyrylbenzene Derivatives as Potential Therapeutic and Imaging Agents for Soluble and Insoluble Amyloid β Aggregates in Alzheimer's Disease.Journal of the American Chemical Society · 2021Article
- Design of a multivalent bifunctional chelator for diagnosticProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Metals in Imaging of Alzheimer's Disease.International journal of molecular sciences · 2020Review
- Copper Toxicity Links to Pathogenesis of Alzheimer's Disease and Therapeutics Approaches.International journal of molecular sciences · 2020Review
- Amentoflavone: A Bifunctional Metal Chelator that Controls the Formation of Neurotoxic Soluble AβACS chemical neuroscience · 2020Article
- Rhodamine-Based Metal Chelator: A Potent Inhibitor of Metal-Catalyzed Amyloid Toxicity.ACS omega · 2020Article
- Aryldiazoquinoline based multifunctional small molecules for modulating AβRSC advances · 2020Article
- Metal-chelating benzothiazole multifunctional compounds for the modulation andChemical science · 2020Article
- A Multifunctional Chemical Agent as an Attenuator of Amyloid Burden and Neuroinflammation in Alzheimer's Disease.ACS chemical neuroscience · 2020Article
- Azo-dyes based small bifunctional molecules for metal chelation and controlling amyloid formation.Inorganica chimica acta · 2018Article
- Coordination Chemistry of Bifunctional Chemical Agents Designed for Applications inInorganic chemistry · 2017Article
- Evaluation ofJournal of the American Chemical Society · 2017Article
- Multi-target-directed phenol-triazole ligands as therapeutic agents for Alzheimer's disease.Chemical science · 2017Article
- Development of multifunctional heterocyclic Schiff base as a potential metal chelator: a comprehensive spectroscopic approach towards drug discovery.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Multifunctional metal chelators that can modulate the amyloid β (Aβ) peptide aggregation and its interaction with metal ions such as copper and zinc hold considerable promise as therapeutic agents for Alzheimer's disease (AD). However, specific rather than systemic metal chelation by these compounds is needed in order to limit any side effects. Reported herein are two novel small bifunctional chelators, 2-[2-hydroxy-4-(diethylamino)phenyl]benzothiazole (L1) and 2-(2-hydroxy-3-methoxyphenyl)benzothiazole (L2), in which the metal-binding donor atoms are integrated within a molecular framework derived from the amyloid-binding fluorescent dye thioflavin T (ThT). The metal-binding properties of L1 and L2 were probed by pH spectrophotometric titrations to determine their pKa values and the corresponding metal complex stability constants, and the isolated metal complexes were structurally characterized. The amyloid-fibril-binding properties of L1 and L2 were investigated by fluorescence titrations and ThT competition assays. Interestingly, L1 and L2 do not lead to the formation of neurotoxic Aβ42 oligomers in the presence or absence of metal ions, as observed by native gel electrophoresis, Western blotting, and transmission electron microscopy. In addition, L1 and L2 were able to reduce the cell toxicity of preformed Aβ42 oligomers and of the copper-stabilized Aβ42 oligomers. Given their ability to reduce the toxicity of soluble Aβ42 and Cu-Aβ42 species, L1 and L2 are promising lead compounds for the development of chemical agents that can control the neurotoxicity of soluble Aβ42 species in AD.
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