ArticleACS chemical biology2014
De novo design of self-assembling foldamers that inhibit heparin-protein interactions.
Article in ACS chemical biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 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
12 citing papers in PubMed, 41 citations in OpenAlex.
- Betaine-Conjugated ß-Peptide Foldamers: Influence of Quaternary Charge on Self-Organization and MorphologyFormation.ChemistryOpen · 2025Article
- Article
- Comparative Study of Molecular Mechanics Force Fields for β-Peptidic Foldamers: Folding and Self-Association.Journal of chemical information and modeling · 2023Article
- Roles of Metal Ions in Foldamers and Other Conformationally Flexible Supramolecular Systems.ACS organic & inorganic Au · 2022Review
- Dynamic Combinatorial Optimization ofJournal of medicinal chemistry · 2022Article
- Membrane active Janus-oligomers of βChemical science · 2020Article
- Article
- Targeting heparin and heparan sulfate protein interactions.Organic & biomolecular chemistry · 2017Review
- Electrostatic binding of polyanions using self-assembled multivalent (SAMul) ligand displays - structure-activity effects on DNA/heparin binding.Chemical science · 2016Article
- Cationic Peptides and Peptidomimetics Bind Glycosaminoglycans as Potential Sema3A Pathway Inhibitors.Biophysical journal · 2016Article
- Small molecule antagonists of cell-surface heparan sulfate and heparin-protein interactions.Chemical science · 2015Article
- Specific aromatic foldamers potently inhibit spontaneous and seeded Aβ42 and Aβ43 fibril assembly.The Biochemical journal · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors at 2 institutions in 1 country.
Funding
Abstract
A series of self-associating foldamers have been designed as heparin reversal agents, as antidotes to prevent bleeding due to this potent antithrombotic agent. The foldamers have a repeating sequence of Lys-Sal, in which Sal is 5-amino-2-methoxy-benzoic acid. These foldamers are designed to self-associate along one face of an extended chain in a β-sheet-like interaction. The methoxy groups were included to form intramolecular hydrogen bonds that preclude the formation of very large amyloid-like aggregates, while the positively charged Lys side chains were introduced to interact electrostatically with the highly anionic heparin polymer. The prototype compound (Lys-Sal)4 carboxamide weakly associates in aqueous solution at physiological salt concentration in a monomer-dimer-hexamer equilibrium. The association is greatly enhanced at either high ionic strength or in the presence of a heparin derivative, which is bound tightly. Variants of this foldamer are active in an antithrombin III-factor Xa assay, showing their potential as heparin reversal agents.
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What OpenQuestion holds
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.