ArticleChembiochem : a European journal of chemical biology2014
Modulation of amyloid-β aggregation by histidine-coordinating Cobalt(III) Schiff base complexes.
Article in Chembiochem : a European journal of chemical biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 47 citations in OpenAlex.
- Cobalt complexes in biology and medicine: enzymatic functions, pharmacological applications, and health challenges.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2026Review
- Covalent Modulation of Protein Misfolding and Aggregation Processes in the Context of Neurodegenerative Diseases.Archiv der Pharmazie · 2026Review
- Article
- Synthesis and Biological Activities of Some Metal Complexes of Peptides: A Review.Biotech (Basel (Switzerland)) · 2024Review
- Studying Peptide-Metal Ion Complex Structures by Solution-State NMR.International journal of molecular sciences · 2022Review
- Modulation of amyloid-β aggregation by metal complexes with a dual binding mode and their delivery across the blood-brain barrier using focused ultrasound.Chemical science · 2021Article
- Investigating in Vitro Amyloid Peptide 1-42 Aggregation: Impact of Higher Molecular Weight Stable Adducts.ACS omega · 2019Article
- Physical properties, ligand substitution reactions, and biological activity of Co(iii)-Schiff base complexes.Dalton transactions (Cambridge, England : 2003) · 2019Article
- Platinum(II)International journal of molecular sciences · 2019Article
- A catalytic antioxidant for limiting amyloid-beta peptide aggregation and reactive oxygen species generation.Chemical science · 2019Article
- Modification of Aβ Peptide Aggregation via Covalent Binding of a Series of Ru(III) Complexes.Frontiers in chemistry · 2019Article
- 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
- Inhibition of Beta-Amyloid Fibrillation by Luminescent Iridium(III) Complex Probes.Scientific reports · 2015Article
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
Oligomers of the Aβ42 peptide are significant neurotoxins linked to Alzheimer's disease (AD). Histidine (His) residues present at the N terminus of Aβ42 are believed to influence toxicity by either serving as metal-ion binding sites (which promote oligomerization and oxidative damage) or facilitating synaptic binding. Transition metal complexes that bind to these residues and modulate Aβ toxicity have emerged as therapeutic candidates. Cobalt(III) Schiff base complexes (Co-sb) were evaluated for their ability to interact with Aβ peptides. HPLC-MS, NMR, fluorescence, and DFT studies demonstrated that Co-sb complexes could interact with the His residues in a truncated Aβ16 peptide representing the Aβ42 N terminus. Coordination of Co-sb complexes altered the structure of Aβ42 peptides and promoted the formation of large soluble oligomers. Interestingly, this structural perturbation of Aβ correlated to reduced synaptic binding to hippocampal neurons. These results demonstrate the promise of Co-sb complexes in anti-AD therapeutic approaches.
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