ArticleNature communications2016
Foldamer-mediated manipulation of a pre-amyloid toxin.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
What it found
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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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
24 citing papers in PubMed, 77 citations in OpenAlex.
- Prion Protein-Derived Cell-Penetrating Peptide Inhibits Type II Diabetes-Associated Islet Amyloid Polypeptide Aggregation and Cytotoxicity.Biochemistry · 2026Article
- Foldamers rescue synucleinopathy phenotypes in multiple in vitro and in vivo models.Science translational medicine · 2026Article
- Molecular Mechanisms of Islet Amyloid Polypeptide Aggregation: Towards Chemical Strategies to Prevent Amyloid Formation and to Design Non-Aggregating Peptide Therapeutics.International journal of molecular sciences · 2026Review
- Unnatural helical peptidic foldamers as protein segment mimics.Chemical Society reviews · 2023Review
- It's ok to be outnumbered - sub-stoichiometric modulation of homomeric protein complexes.RSC medicinal chemistry · 2023Review
- Foldamers reveal and validate therapeutic targets associated with toxic α-synuclein self-assembly.Nature communications · 2022Article
- Molecular dynamics study of water channels in natural and synthetic amyloid-β fibrils.The Journal of chemical physics · 2021Article
- Natural and Synthetic Oligoarylamides: Privileged Structures for Medical Applications.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Review
- Defining the Neuropathological Aggresome acrossThe journal of physical chemistry. B · 2021Review
- Optimal anchoring of a foldamer inhibitor of ASF1 histone chaperone through backbone plasticity.Science advances · 2021Article
- Applications of Discrete Synthetic Macromolecules in Life and Materials Science: Recent and Future Trends.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2021Review
- Proteostasis of Islet Amyloid Polypeptide: A Molecular Perspective of Risk Factors and Protective Strategies for Type II Diabetes.Chemical reviews · 2021Review
- Visualizing and trapping transient oligomers in amyloid assembly pathways.Biophysical chemistry · 2021Review
- Aromatic Foldamer Helices as α-Helix Extended Surface Mimetics.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020Article
- Sub-stoichiometric inhibition of IAPP aggregation: a peptidomimetic approach to anti-amyloid agents.RSC chemical biology · 2020Article
- Secondary structures and cell-penetrating abilities of arginine-rich peptide foldamers.Scientific reports · 2019Article
- Role and Cytotoxicity of Amylin and Protection of Pancreatic Islet β-Cells from Amylin Cytotoxicity.Cells · 2018Review
- IAPP/amylin and β-cell failure: implication of the risk factors of type 2 diabetes.Diabetology international · 2018Article
- Conformational switching within dynamic oligomers underpins toxic gain-of-function by diabetes-associated amyloid.Nature communications · 2018Article
- Small molecule probes of protein aggregation.Current opinion in chemical biology · 2017Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Disordered proteins, such as those central to Alzheimer's and Parkinson's, are particularly intractable for structure-targeted therapeutic design. Here we demonstrate the capacity of a synthetic foldamer to capture structure in a disease relevant peptide. Oligoquinoline amides have a defined fold with a solvent-excluded core that is independent of its outwardly projected, derivatizable moieties. Islet amyloid polypeptide (IAPP) is a peptide central to β-cell pathology in type II diabetes. A tetraquinoline is presented that stabilizes a pre-amyloid, α-helical conformation of IAPP. This charged, dianionic compound is readily soluble in aqueous buffer, yet crosses biological membranes without cellular assistance: an unexpected capability that is a consequence of its ability to reversibly fold. The tetraquinoline docks specifically with intracellular IAPP and rescues β-cells from toxicity. Taken together, our work here supports the thesis that stabilizing non-toxic conformers of a plastic protein is a viable strategy for cytotoxic rescue addressable using oligoquinoline amides.
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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.