ArticleJournal of the American Chemical Society2011
Macrocyclic β-sheet peptides that inhibit the aggregation of a tau-protein-derived hexapeptide.
Article in Journal of the American Chemical Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 54 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
54 citing papers in PubMed, 123 citations in OpenAlex.
- Thermodynamic Frontiers in Hemoglobin-Inspired Polymer Science for Diagnosis and Modulation of Neurodegenerative Diseases.Cell biochemistry and function · 2026Review
- Discovery of SHANK1-PDZ Peptide-Fragment Inhibitors Using a Dynamic Ligation Screening Strategy.Biochemistry · 2026Article
- Consequences of Peptide Macrocyclization Revealed by Virus-Inspired β-Hairpin Mimetics.ACS chemical biology · 2026Article
- Alzheimer's Disease: From Molecular Mechanisms to Promising Therapeutic Strategies.International journal of molecular sciences · 2025Review
- β-Bracelets: Macrocyclic Cross-β Epitope Mimics Based on a Tau Conformational Strain.Journal of the American Chemical Society · 2023Article
- Structure-based design of nanobodies that inhibit seeding of Alzheimer's patient-extracted tau fibrils.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Multipronged diagnostic and therapeutic strategies for Alzheimer's disease.Chemical science · 2022Review
- Three-repeat and four-repeat tau isoforms form different oligomers.Protein science : a publication of the Protein Society · 2022Article
- A novel D-amino acid peptide with therapeutic potential (ISAD1) inhibits aggregation of neurotoxic disease-relevant mutant Tau and prevents Tau toxicity in vitro.Alzheimer's research & therapy · 2022Article
- Potent Tau Aggregation Inhibitor D-Peptides Selected against Tau-Repeat 2 Using Mirror Image Phage Display.Chembiochem : a European journal of chemical biology · 2021Article
- N-Amination Converts Amyloidogenic Tau Peptides into Soluble Antagonists of Cellular Seeding.ACS chemical neuroscience · 2021Article
- The Structure Biology of Tau and Clue for Aggregation Inhibitor Design.The protein journal · 2021Review
- Antimicrobial α-defensins as multi-target inhibitors against amyloid formation and microbial infection.Chemical science · 2021Article
- Amyloid-β-Derived Peptidomimetics Inhibits Tau Aggregation.ACS omega · 2021Article
- A theoretical study of polymorphism in VQIVYK fibrils.Biophysical journal · 2021Article
- Structural Characterization of Receptor-Receptor Interactions in the Allosteric Modulation of G Protein-Coupled Receptor (GPCR) Dimers.International journal of molecular sciences · 2021Review
- The structure and phase of tau: from monomer to amyloid filament.Cellular and molecular life sciences : CMLS · 2021Review
- Arginine and Arginine-Rich Peptides as Modulators of Protein Aggregation and Cytotoxicity Associated With Alzheimer's Disease.Frontiers in molecular neuroscience · 2021Review
- Asparagine residue 368 is involved in Alzheimer's disease tau strain-specific aggregation.The Journal of biological chemistry · 2020Article
- Controlled Lengthwise Assembly of Helical Peptide Nanofibers to Modulate CD8Advanced materials (Deerfield Beach, Fla.) · 2020Article
Corrections and comments
- Erratum issued
Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
This paper describes studies of a series of macrocyclic β-sheet peptides 1 that inhibit the aggregation of a tau-protein-derived peptide. The macrocyclic β-sheet peptides comprise a pentapeptide "upper" strand, two δ-linked ornithine turn units, and a "lower" strand comprising two additional residues and the β-sheet peptidomimetic template "Hao". The tau-derived peptide Ac-VQIVYK-NH(2) (AcPHF6) aggregates in solution through β-sheet interactions to form straight and twisted filaments similar to those formed by tau protein in Alzheimer's neurofibrillary tangles. Macrocycles 1 containing the pentapeptide VQIVY in the "upper" strand delay and suppress the onset of aggregation of the AcPHF6 peptide. Inhibition is particularly pronounced in macrocycles 1a, 1d, and 1f, in which the two residues in the "lower" strand provide a pattern of hydrophobicity and hydrophilicity that matches that of the pentapeptide "upper" strand. Inhibition varies strongly with the concentration of these macrocycles, suggesting that it is cooperative. Macrocycle 1b containing the pentapeptide QIVYK shows little inhibition, suggesting the possibility of a preferred direction of growth of AcPHF6 β-sheets. On the basis of these studies, a model is proposed in which the AcPHF6 amyloid grows as a layered pair of β-sheets and in which growth is blocked by a pair of macrocycles that cap the growing paired hydrogen-bonding edges. This model provides a provocative and appealing target for future inhibitor design.
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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.