ArticleThe Journal of biological chemistry2015
Structural Mechanism of the Interaction of Alzheimer Disease Aβ Fibrils with the Non-steroidal Anti-inflammatory Drug (NSAID) Sulindac Sulfide.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 31 citations in OpenAlex.
- In vitro, cellular and in vivo studies of amyloid oligomers structure and toxicity: Challenges and advances.Protein science : a publication of the Protein Society · 2026Review
- Targeting the awry Aβ pathway in Alzheimer's disease: hype and hurdles.Inflammopharmacology · 2025Review
- Segmental Dynamics of Membranous Cholesterol are Coupled.Journal of the American Chemical Society · 2023Article
- Controlling amyloid formation of intrinsically disordered proteins and peptides: slowing down or speeding up?Essays in biochemistry · 2022Article
- The clinical drug candidate anle138b binds in a cavity of lipidic α-synuclein fibrils.Nature communications · 2022Article
- Binding Sites of a Positron Emission Tomography Imaging Agent in Alzheimer's β-Amyloid Fibrils Studied UsingJournal of the American Chemical Society · 2022Article
- Sulfur-containing therapeutics in the treatment of Alzheimer's disease.Medicinal chemistry research : an international journal for rapid communications on design and mechanisms of action of biologically active agents · 2021Article
- Solid-state NMR spectroscopy.Nature reviews. Methods primers · 2021Article
- Mapping the Binding Interface of PET Tracer Molecules and Alzheimer Disease Aβ Fibrils by Using MAS Solid-State NMR Spectroscopy.Chembiochem : a European journal of chemical biology · 2020Article
- Structural Insight into IAPP-Derived Amyloid Inhibitors and Their Mechanism of Action.Angewandte Chemie (International ed. in English) · 2020Article
- Two decades of progress in structural and dynamic studies of amyloids by solid-state NMR.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2019Review
- Current Progress on Peroxisome Proliferator-activated Receptor Gamma Agonist as an Emerging Therapeutic Approach for the Treatment of Alzheimer's Disease: An Update.Current neuropharmacology · 2019Review
- Article
- Curcumin Dictates Divergent Fates for the Central Salt Bridges in Amyloid-βBiophysical journal · 2017Article
- Fast Motions of Key Methyl Groups in Amyloid-β Fibrils.Biophysical journal · 2016Article
- Enhancing NMR Sensitivity of Natural-Abundance Low-γ Nuclei by Ultrafast Magic-Angle-Spinning Solid-State NMR Spectroscopy.Chemphyschem : a European journal of chemical physics and physical chemistry · 2016Article
- Flexibility and Solvation of Amyloid-β Hydrophobic Core.The Journal of biological chemistry · 2016Article
- Structural Polymorphism of Alzheimer's β-Amyloid Fibrils as Controlled by an E22 Switch: A Solid-State NMR Study.Journal of the American Chemical Society · 2016Article
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Authors and funding
8 authors at 6 institutions in 3 countries.
Funding
Abstract
Alzheimer disease is the most severe neurodegenerative disease worldwide. In the past years, a plethora of small molecules interfering with amyloid-β (Aβ) aggregation has been reported. However, their mode of interaction with amyloid fibers is not understood. Non-steroidal anti-inflammatory drugs (NSAIDs) are known γ-secretase modulators; they influence Aβ populations. It has been suggested that NSAIDs are pleiotrophic and can interact with more than one pathomechanism. Here we present a magic angle spinning solid-state NMR study demonstrating that the NSAID sulindac sulfide interacts specifically with Alzheimer disease Aβ fibrils. We find that sulindac sulfide does not induce drastic architectural changes in the fibrillar structure but intercalates between the two β-strands of the amyloid fibril and binds to hydrophobic cavities, which are found consistently in all analyzed structures. The characteristic Asp(23)-Lys(28) salt bridge is not affected upon interacting with sulindac sulfide. The primary binding site is located in the vicinity of residue Gly(33), a residue involved in Met(35) oxidation. The results presented here will assist the search for pharmacologically active molecules that can potentially be employed as lead structures to guide the design of small molecules for the treatment of Alzheimer disease.
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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.