ArticleJournal of the American Chemical Society2014
A fibril-like assembly of oligomers of a peptide derived 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 13 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
13 citing papers in PubMed, 34 citations in OpenAlex.
- A β-hairpin peptide derived from Aβ forms different oligomers in the crystal state and in aqueous solution.Organic & biomolecular chemistry · 2025Article
- Phototherapeutic effect of transformable peptides containing pheophorbide a on colorectal cancer.Drug delivery · 2022Article
- Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer's Disease, Parkinson's Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis.Chemical reviews · 2021Review
- Target-driven supramolecular self-assembly for selective amyloid-β photooxygenation against Alzheimer's disease.Chemical science · 2020Article
- A Novel PEGylated Block Copolymer in New Age Therapeutics for Alzheimer's Disease.Molecular neurobiology · 2019Article
- Somatostatin binds to the human amyloid β peptide and favors the formation of distinct oligomers.eLife · 2017Article
- POSS-Appended Diphenylalanine: Self-Cleaning, Pollution-Protective, and Fire-Retardant Hybrid Molecular Material.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
- 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
- Comparison of design strategies for α-helix backbone modification in a protein tertiary fold.Chemical communications (Cambridge, England) · 2016Article
- Brazilin inhibits amyloid β-protein fibrillogenesis, remodels amyloid fibrils and reduces amyloid cytotoxicity.Scientific reports · 2015Article
- Synthetic Peptides as Protein Mimics.Frontiers in bioengineering and biotechnology · 2015Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
A macrocyclic β-sheet peptide containing two nonapeptide segments based on Aβ(15-23) (QKLVFFAED) forms fibril-like assemblies of oligomers in the solid state. The X-ray crystallographic structure of macrocyclic β-sheet peptide 3 was determined at 1.75 Å resolution. The macrocycle forms hydrogen-bonded dimers, which further assemble along the fibril axis in a fashion resembling a herringbone pattern. The extended β-sheet comprising the dimers is laminated against a second layer of dimers through hydrophobic interactions to form a fibril-like assembly that runs the length of the crystal lattice. The second layer is offset by one monomer subunit, so that the fibril-like assembly is composed of partially overlapping dimers, rather than discrete tetramers. In aqueous solution, macrocyclic β-sheet 3 and homologues 4 and 5 form discrete tetramers, rather than extended fibril-like assemblies. The fibril-like assemblies of oligomers formed in the solid state by macrocyclic β-sheet 3 represent a new mode of supramolecular assembly not previously observed for the amyloidogenic central region of Aβ. The structures observed at atomic resolution for this peptide model system may offer insights into the structures of oligomers and oligomer assemblies formed by full-length Aβ and may provide a window into the propagation and replication of amyloid oligomers.
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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.