ArticleChembiochem : a European journal of chemical biology2020
Mapping the Binding Interface of PET Tracer Molecules and Alzheimer Disease Aβ Fibrils by Using MAS Solid-State NMR Spectroscopy.
Article in Chembiochem : a European journal of chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 14 citations in OpenAlex.
- PET imaging of alpha-synuclein: from radiotracer design through in vitro and in vivo translation.European journal of nuclear medicine and molecular imaging · 2026Review
- Molecular design of MRI probes for targeting amyloid-β species: fromTheranostics · 2026Review
- The clinical drug candidate anle138b binds in a cavity of lipidic α-synuclein fibrils.Nature communications · 2022Article
- Site-specific protein methyl deuterium quadrupolar patterns by proton-detected 3DJournal of biomolecular NMR · 2022Article
- Binding Sites of a Positron Emission Tomography Imaging Agent in Alzheimer's β-Amyloid Fibrils Studied UsingJournal of the American Chemical Society · 2022Article
- Toward Novel [Frontiers in aging neuroscience · 2022Article
- Maximizing efficiency of dipolar recoupling in solid-state NMR using optimal control sequences.Science advances · 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
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Positron emission tomography (PET) tracer molecules like thioflavin T specifically recognize amyloid deposition in brain tissue by selective binding to hydrophobic or aromatic surface grooves on the β-sheet surface along the fibril axis. The molecular basis of this interaction is, however, not well understood. We have employed magic angle spinning (MAS) solid-state NMR spectroscopy to characterize Aβ-PET tracer complexes at atomic resolution. We established a titration protocol by using bovine serum albumin as a carrier to transfer hydrophobic small molecules to Aβ(1-40) fibrillar aggregates. The same Aβ(1-40) amyloid fibril sample was employed in subsequent titrations to minimize systematic errors that potentially arise from sample preparation. In the experiments, the small molecules
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