ArticleJournal of the American Chemical Society2016
X-ray Crystallographic Structures of a Trimer, Dodecamer, and Annular Pore Formed by an Aβ17-36 β-Hairpin.
Article in Journal of the American Chemical Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed.
- The Influence of POPC as a Coaggregate in Amyloid-β Oligomer Formation.ACS chemical neuroscience · 2025Article
- The role of hydrophobic collapse in cytotoxic and functional amyloid oligomerization.Biophysical journal · 2025Article
- A β-hairpin peptide derived from Aβ forms different oligomers in the crystal state and in aqueous solution.Organic & biomolecular chemistry · 2025Article
- α-Methylation Enables the X-ray Crystallographic Observation of Oligomeric Assemblies Formed by a β-Hairpin Peptide Derived from Aβ.The Journal of organic chemistry · 2025Article
- Structures of Oligomeric States of Tau Protein, Amyloid-β, α-Synuclein and Prion Protein Implicated in Alzheimer's Disease, Parkinson's Disease and Prionopathies.International journal of molecular sciences · 2024Review
- Dataset from a human-in-the-loop approach to identify functionally important protein residues from literature.Scientific data · 2024Article
- A turn for the worse: Aβ β-hairpins in Alzheimer's disease.Bioorganic & medicinal chemistry · 2024Review
- Antibodies Raised Against an Aβ Oligomer Mimic Recognize Pathological Features in Alzheimer's Disease and Associated Amyloid-Disease Brain Tissue.ACS central science · 2024Article
- A β-barrel-like tetramer formed by a β-hairpin derived from Aβ.Chemical science · 2023Article
- A Hybrid Structural Method for Investigating Low Molecular Weight Oligomeric Structures of Amyloid Beta.Chembiochem : a European journal of chemical biology · 2022Article
- Effects of Familial Alzheimer's Disease Mutations on the Assembly of a β-Hairpin Peptide Derived from AβBiochemistry · 2022Article
- A Disulfide-Stabilized Aβ that Forms Dimers but Does Not Form Fibrils.Biochemistry · 2022Article
- An Improved Turn Structure for Inducing β-Hairpin Formation in Peptides.Angewandte Chemie (International ed. in English) · 2021Article
- Exploring amyloid oligomers with peptide model systems.Current opinion in chemical biology · 2021Review
- Structural Studies Providing Insights into Production and Conformational Behavior of Amyloid-β Peptide Associated with Alzheimer's Disease Development.Molecules (Basel, Switzerland) · 2021Review
- The biogenesis and biology of amyloid β oligomers in the brain.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2020Review
- X-ray Crystallography Reveals Parallel and Antiparallel β-Sheet Dimers of a β-Hairpin Derived from AβACS chemical neuroscience · 2020Article
- Effects of N-Terminal Residues on the Assembly of Constrained β-Hairpin Peptides Derived from Aβ.Journal of the American Chemical Society · 2020Article
- Small molecule-mediated co-assembly of amyloid-β oligomers reduces neurotoxicity through promoting non-fibrillar aggregation.Chemical science · 2020Article
- High-Speed Atomic Force Microscopy Reveals the Structural Dynamics of the Amyloid-β and Amylin Aggregation Pathways.International journal of molecular sciences · 2020Review
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
High-resolution structures of oligomers formed by the β-amyloid peptide Aβ are needed to understand the molecular basis of Alzheimer's disease and develop therapies. This paper presents the X-ray crystallographic structures of oligomers formed by a 20-residue peptide segment derived from Aβ. The development of a peptide in which Aβ17-36 is stabilized as a β-hairpin is described, and the X-ray crystallographic structures of oligomers it forms are reported. Two covalent constraints act in tandem to stabilize the Aβ17-36 peptide in a hairpin conformation: a δ-linked ornithine turn connecting positions 17 and 36 to create a macrocycle and an intramolecular disulfide linkage between positions 24 and 29. An N-methyl group at position 33 blocks uncontrolled aggregation. The peptide readily crystallizes as a folded β-hairpin, which assembles hierarchically in the crystal lattice. Three β-hairpin monomers assemble to form a triangular trimer, four trimers assemble in a tetrahedral arrangement to form a dodecamer, and five dodecamers pack together to form an annular pore. This hierarchical assembly provides a model, in which full-length Aβ transitions from an unfolded monomer to a folded β-hairpin, which assembles to form oligomers that further pack to form an annular pore. This model may provide a better understanding of the molecular basis of Alzheimer's disease at atomic resolution.
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