ArticleJournal of the American Chemical Society2015
High resolution structural characterization of Aβ42 amyloid fibrils by magic angle spinning NMR.
Article in Journal of the American Chemical Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.
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Who cites it
64 citing papers in PubMed.
- High-frequency dynamic nuclear polarization in rotating solids.Science advances · 2026Review
- Use of high-affinity scFv antibody NUsc1 for isolation and sensitive detection of Alzheimer's-associated amyloid beta oligomers.The Journal of biological chemistry · 2026Article
- Design and commissioning of a new synchrotron beamline dedicated to X-ray footprinting mass spectrometry.Journal of synchrotron radiation · 2026Article
- Higher Magnetic Field NMR Renders Resolution Enhancement on Ganglioside GD3 Catalyzed AβbioRxiv : the preprint server for biology · 2026Article
- Aducanumab binding to AβProceedings of the National Academy of Sciences of the United States of America · 2025Article
- MAS Cryoprobe Enhances Solid-State NMR Signals of α-Synuclein Fibrils.bioRxiv : the preprint server for biology · 2025Article
- Aducanumab Binding to AβbioRxiv : the preprint server for biology · 2025Article
- Proton-Detected Solid-State NMR for Deciphering Structural Polymorphism and Dynamic Heterogeneity of Cellular Carbohydrates in Pathogenic Fungi.Journal of the American Chemical Society · 2025Article
- Structural convergence and membrane interactions of AβCommunications chemistry · 2025Article
- The Flipons, Infections, and Amyloids that Foreshadow the Fading Memories of Alzheimer's Disease.Neuroscience insights · 2025Review
- Dipolar Recoupling in Rotating Solids.Chemical reviews · 2024Review
- E22G Aβ40 fibril structure and kinetics illuminate how Aβ40 rather than Aβ42 triggers familial Alzheimer's.Nature communications · 2024Article
- Evidence for SbioRxiv : the preprint server for biology · 2024Article
- Structural characterization of E22G AβPhysical chemistry chemical physics : PCCP · 2024Article
- Structural Consequences of Introducing Bioactive Domains to Designer β-Sheet Peptide Self-Assemblies.Biomacromolecules · 2024Article
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- Self-Assembling Peptides with Insulin-Like Growth Factor Mimicry.ACS applied materials & interfaces · 2024Article
- Thermochromic Behavior of Polydiacetylene Nanomaterials Driven by Charged Peptide Amphiphiles.Biomacromolecules · 2023Article
- A Hybrid Structural Method for Investigating Low Molecular Weight Oligomeric Structures of Amyloid Beta.Chembiochem : a European journal of chemical biology · 2022Article
- Impact of Aβ40 and Aβ42 Fibrils on the Transcriptome of Primary Astrocytes and Microglia.Biomedicines · 2022Article
4 more citing papers are in PubMed but not listed here.
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6 authors.
Funding
Abstract
The presence of amyloid plaques composed of amyloid beta (Aβ) fibrils is a hallmark of Alzheimer's disease (AD). The Aβ peptide is present as several length variants with two common alloforms consisting of 40 and 42 amino acids, denoted Aβ1-40 and Aβ1-42, respectively. While there have been numerous reports that structurally characterize fibrils of Aβ1-40, very little is known about the structure of amyloid fibrils of Aβ1-42, which are considered the more toxic alloform involved in AD. We have prepared isotopically (13)C/(15)N labeled AβM01-42 fibrils in vitro from recombinant protein and examined their (13)C-(13)C and (13)C-(15)N magic angle spinning (MAS) NMR spectra. In contrast to several other studies of Aβ fibrils, we observe spectra with excellent resolution and a single set of chemical shifts, suggesting the presence of a single fibril morphology. We report the initial structural characterization of AβM01-42 fibrils utilizing (13)C and (15)N shift assignments of 38 of the 43 residues, including the backbone and side chains, obtained through a series of cross-polarization based 2D and 3D (13)C-(13)C, (13)C-(15)N MAS NMR experiments for rigid residues along with J-based 2D TOBSY experiments for dynamic residues. We find that the first ∼5 residues are dynamic and most efficiently detected in a J-based TOBSY spectrum. In contrast, residues 16-42 are easily observed in cross-polarization experiments and most likely form the amyloid core. Calculation of ψ and φ dihedral angles from the chemical shift assignments indicate that 4 β-strands are present in the fibril's secondary structure.
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