ArticleACS chemical neuroscience2021
N-Amination Converts Amyloidogenic Tau Peptides into Soluble Antagonists of Cellular Seeding.
Article in ACS chemical neuroscience, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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
8 citing papers in PubMed, 12 citations in OpenAlex.
- Fluctuating β-Sheet Secondary Structure in DS119 Explains the Small Effects of Backbone N-Amination on Thermal Stability.Journal of peptide science : an official publication of the European Peptide Society · 2026Article
- N-Amino Peptide-Graphene Quantum Dot Loaded Small Extracellular Vesicles for Targeted Therapy of Tauopathies.Advanced nanobiomed research · 2025Article
- Beyond N-Alkylation: Synthesis, Structure, and Function of N-Amino Peptides.Accounts of chemical research · 2024Article
- β-Bracelets: Macrocyclic Cross-β Epitope Mimics Based on a Tau Conformational Strain.Journal of the American Chemical Society · 2023Article
- Harnessing Aromatic-Histidine Interactions through Synergistic Backbone Extension and Side Chain Modification.Angewandte Chemie (International ed. in English) · 2023Article
- Blocking tau transmission by biomimetic graphene nanoparticles.Journal of materials chemistry. B · 2023Article
- Backbone N-Amination Promotes the Folding of β-Hairpin Peptides via a Network of Hydrogen Bonds.Journal of chemical information and modeling · 2022Article
- Protein condensation diseases: therapeutic opportunities.Nature communications · 2022Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The spread of neurofibrillary tangles composed of tau protein aggregates is a hallmark of Alzheimer's and related neurodegenerative diseases. Early oligomerization of tau involves conformational reorganization into parallel β-sheet structures and supramolecular assembly into toxic fibrils. Despite the need for selective inhibitors of tau propagation, β-rich protein assemblies are inherently difficult to target with small molecules. Here, we describe a minimalist approach to mimic the aggregation-prone modules within tau. We carried out a backbone residue scan and show that amide N-amination completely abolishes the tendency of these peptides to self-aggregate, rendering them soluble mimics of ordered β-strands from the tau R2 and R3 domains. Several N-amino peptides (NAPs) inhibit tau fibril formation in vitro. We further demonstrate that NAPs
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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.