ArticleChemical communications (Cambridge, England)2016
Foldamer scaffolds suggest distinct structures are associated with alternative gains-of-function in a preamyloid toxin.
Article in Chemical communications (Cambridge, England), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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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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
6 citing papers in PubMed.
- Rationally Designed Pentapeptide Analogs of Aβ19-23 Fragment as Potent Inhibitors of Aβ42 Aggregation.Molecules (Basel, Switzerland) · 2025Article
- Inhibition of Phosphorylated Alpha-Synuclein Aggregation by Synthetic Protein Mimetics and Foldamers.ACS chemical neuroscience · 2025Article
- Foldamers reveal and validate therapeutic targets associated with toxic α-synuclein self-assembly.Nature communications · 2022Article
- Natural and Synthetic Oligoarylamides: Privileged Structures for Medical Applications.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Review
- Amyloid Proteins and Peripheral Neuropathy.Cells · 2020Review
- Conformational switching within dynamic oligomers underpins toxic gain-of-function by diabetes-associated amyloid.Nature communications · 2018Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
An oligoquinoline foldamer library was synthesized and screened for antagonism of lipid bilayer catalysed assembly of islet amyloid polypeptide (IAPP). One tetraquinoline, ADM-116, showed exceptional potency not only in this assay, but also in secondary assays measuring lipid bilayer integrity and rescue of insulin secreting cells from the toxic effects of IAPP. Structure activity studies identified three additional oligoquinolines, closely related to ADM-116, which also have strong activity in the primary, but not the secondary assays. This contrasts work using an oligopyrdyl foldamer scaffold in which all three assays are observed to be correlated. The results suggest that while there is commonality to the structures and pathways of IAPP conformational change, it is nevertheless possible to leverage foldamers to separately affect IAPP's alternative gains-of-function.
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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.