ArticleJournal of the American Chemical Society2014
Polymorphism of oligomers of a peptide from β-amyloid.
Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 29 citations in OpenAlex.
- Endogenous Aβ and Exogenous Wheat Gluten Nanostructures: Understanding Peptide Self-Assembly in Disease.ACS nano · 2025Review
- A β-hairpin peptide derived from Aβ forms different oligomers in the crystal state and in aqueous solution.Organic & biomolecular chemistry · 2025Article
- Gas-Phase Unfolding of Protein Complexes Distinguishes Conformational Isomers.Journal of the American Chemical Society · 2022Article
- A Disulfide-Stabilized Aβ that Forms Dimers but Does Not Form Fibrils.Biochemistry · 2022Article
- Amyloid Evolution: Antiparallel Replaced by Parallel.Biophysical journal · 2020Article
- High-resolution probing of early events in amyloid-β aggregation related to Alzheimer's disease.Chemical communications (Cambridge, England) · 2020Review
- Structural Interaction of Apolipoprotein A-I Mimetic Peptide with Amyloid-β Generates Toxic Hetero-oligomers.Journal of molecular biology · 2020Article
- Structural Heterogeneity in the Preamyloid Oligomers of β-2-Microglobulin.Journal of molecular biology · 2020Article
- Using chirality to probe the conformational dynamics and assembly of intrinsically disordered amyloid proteins.Scientific reports · 2017Article
- A Tetramer Derived from Islet Amyloid Polypeptide.The Journal of organic chemistry · 2017Article
- Study of Molecular Mechanisms of α-Synuclein Assembly: Insight into a Cross-β Structure in the N-Termini of New α-Synuclein Fibrils.ACS omega · 2017Article
- Coassembly of Peptides Derived from β-Sheet Regions of β-Amyloid.Journal of the American Chemical Society · 2016Article
- Assembly of Peptides Derived from β-Sheet Regions of β-Amyloid.Journal of the American Chemical Society · 2016Article
- An Atomistic View of Amyloidogenic Self-assembly: Structure and Dynamics of Heterogeneous Conformational States in the Pre-nucleation Phase.Scientific reports · 2016Article
- X-ray Crystallographic Structure of Oligomers Formed by a Toxic β-Hairpin Derived from α-Synuclein: Trimers and Higher-Order Oligomers.Journal of the American Chemical Society · 2016Article
- Probing of Amyloid Aβ (14-23) Trimers by Single-Molecule Force Spectroscopy.Jacobs journal of molecular and translational medicine · 2016Article
- A fibril-like assembly of oligomers of a peptide derived from β-amyloid.Journal of the American Chemical Society · 2014Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
This contribution reports solution-phase structural studies of oligomers of a family of peptides derived from the β-amyloid peptide (Aβ). We had previously reported the X-ray crystallographic structures of the oligomers and oligomer assemblies formed in the solid state by a macrocyclic β-sheet peptide containing the Aβ(15-23) nonapeptide. In the current study, we set out to determine its assembly in aqueous solution. In the solid state, macrocyclic β-sheet peptide 1 assembles to form hydrogen-bonded dimers that further assemble in a sandwich-like fashion to form tetramers through hydrophobic interactions between the faces bearing V18 and F20. In aqueous solution, macrocyclic β-sheet peptide 1 and homologue 2a form hydrogen-bonded dimers that assemble to form tetramers through hydrophobic interactions between the faces bearing L17, F19, and A21. In the solid state, the hydrogen-bonded dimers are antiparallel, and the β-strands are fully aligned, with residues 17-23 of one of the macrocycles aligned with residues 23-17 of the other. In solution, residues 17-23 of the hydrogen-bonded dimers are shifted out of alignment by two residues toward the C-termini. The two hydrogen-bonded dimers are nearly orthogonal in the solid state, while in solution the dimers are only slightly rotated. The differing morphology of the solution-state and solid-state tetramers is significant, because it may provide a glimpse into some of the structural bases for polymorphism among Aβ oligomers in Alzheimer's disease.
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Registered trials
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