ArticleThe Journal of biological chemistry2014
Curcumin alters the salt bridge-containing turn region in amyloid β(1-42) aggregates.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 65 citations in OpenAlex.
- Interactions Between Nutraceuticals and α-Synuclein Conformational States: Molecular Mechanisms and Neuroprotective Implications in Parkinson's Disease.International journal of molecular sciences · 2026Review
- Exploring the Impact of Curcumin and Carbon Nanotubes on Beta-amyloid Peptide Dimer: Insights from Molecular Dynamics Simulation and Density Functional Theory Methods.Current pharmaceutical biotechnology · 2026Article
- Modulation of AβJournal of chemical information and modeling · 2025Article
- Small-Molecule Inhibitors of Amyloid Beta: Insights from Molecular Dynamics-Part B: Natural Compounds.Pharmaceuticals (Basel, Switzerland) · 2025Review
- Research Mechanism and Progress of the Natural Compound Curcumin in Treating Alzheimer´s Disease.Mini reviews in medicinal chemistry · 2024Review
- Neuro-Nutraceutical Polyphenols: How Far Are We?Antioxidants (Basel, Switzerland) · 2023Review
- Interdisciplinary Approaches to Deal with Alzheimer's Disease-From Bench to Bedside: What Feasible Options Do Already Exist Today?Biomedicines · 2022Review
- Article
- Post-Ischemic Brain Neurodegeneration in the Form of Alzheimer's Disease Proteinopathy: Possible Therapeutic Role of Curcumin.Nutrients · 2022Review
- Miracle fruit seed as a potential supplement for the treatment of learning and memory disorders in Alzheimer's disease.Frontiers in pharmacology · 2022Article
- Exploring the Therapeutic Potential of Phytochemicals in Alzheimer's Disease: Focus on Polyphenols and Monoterpenes.Frontiers in pharmacology · 2022Review
- Structural Arrangement within a Peptide Fibril Derived from the Glaucoma-Associated Myocilin Olfactomedin Domain.The journal of physical chemistry. B · 2021Article
- The Effect of (-)-Epigallocatechin-3-Gallate on the Amyloid-β Secondary Structure.Biophysical journal · 2020Article
- Acetylation of AβACS chemical neuroscience · 2020Article
- Substantiation for the Use of Curcumin during the Development of Neurodegeneration after Brain Ischemia.International journal of molecular sciences · 2020Review
- Renal expression of JAK2 is high in polycystic kidney disease and its inhibition reduces cystogenesis.Scientific reports · 2019Article
- Formulations of Curcumin Nanoparticles for Brain Diseases.Biomolecules · 2019Review
- A Bird's-Eye View of the Multiple Biochemical Mechanisms that Propel Pathology of Alzheimer's Disease: Recent Advances and Mechanistic Perspectives on How to Halt the Disease Progression Targeting Multiple Pathways.Journal of Alzheimer's disease : JAD · 2019Review
- Evaluation of the Antioxidant and Neuroprotectant Activities of New Asymmetrical 1,3-Diketones.Molecules (Basel, Switzerland) · 2018Article
- Insights into protein misfolding and aggregation enabled by solid-state NMR spectroscopy.Solid state nuclear magnetic resonance · 2017Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amyloid β (Aβ) fibrillar deposits in the brain are a hallmark of Alzheimer disease (AD). Curcumin, a common ingredient of Asian spices, is known to disrupt Aβ fibril formation and to reduce AD pathology in mouse models. Understanding the structural changes induced by curcumin can potentially lead to AD pharmaceutical agents with inherent bio-compatibility. Here, we use solid-state NMR spectroscopy to investigate the structural modifications of amyloid β(1-42) (Aβ42) aggregates induced by curcumin. We find that curcumin induces major structural changes in the Asp-23-Lys-28 salt bridge region and near the C terminus. Electron microscopy shows that the Aβ42 fibrils are disrupted by curcumin. Surprisingly, some of these alterations are similar to those reported for Zn(2+) ions, another agent known to disrupt the fibrils and alter Aβ42 toxicity. Our results suggest the existence of a structurally related family of quasi-fibrillar conformers of Aβ42, which is stabilized both by curcumin and by Zn(2+.)
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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.