ArticleBioorganic & medicinal chemistry letters2015
High affinity binding of conformationally constrained synthetic oligomers to an antigen-specific antibody: Discovery of a diagnostically useful synthetic ligand for murine Type 1 diabetes autoantibodies.
Article in Bioorganic & medicinal chemistry letters, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers, 1 of them a synthesis that pooled it.
What it found
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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
8 citing papers in PubMed, 1 synthesis or guideline pooled it, 17 citations in OpenAlex.
- Amyloid Biomarkers in Conformational Diseases at Face Value: A Systematic Review.Molecules (Basel, Switzerland) · 2017Pooled it
- Exploiting Avidity Effects for the Discovery of Low Affinity Protein-Binding Fragments.Journal of medicinal chemistry · 2025Article
- Structural characterization of a peptoid-inspired conformationally constrained oligomer (PICCO) bound to streptavidin.Chemical communications (Cambridge, England) · 2020Article
- Screening one bead one compound libraries against serum using a flow cytometer: Determination of the minimum antibody concentration required for ligand discovery.Bioorganic & medicinal chemistry letters · 2018Article
- Asymmetric synthesis of vinylogous β-amino acids and their incorporation into mixed backbone oligomers.Organic & biomolecular chemistry · 2017Article
- Chemical Tools To Monitor and Manipulate Adaptive Immune Responses.Journal of the American Chemical Society · 2016Review
- Towards vast libraries of scaffold-diverse, conformationally constrained oligomers.Chemical communications (Cambridge, England) · 2016Article
- Reliable diagnosis of murine type 1 diabetes using a panel of autoantigens and "antigen surrogates" mounted onto a liquid array.Molecular bioSystems · 2015Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
'Antigen surrogates' are synthetic, non-natural molecules that recognize the antigen-binding sites of antibodies. These molecules are of interest as replacements for native antigens as antibody 'capture agents' in ELISA-like assays of potential diagnostic utility, for example when the antibody is indicative of a disease state. Antigen surrogates for disease-related antibodies can be mined from one-bead one-compound (OBOC) libraries by first denuding the library of ligands for antibodies present in the serum of control patients or animals, followed by screening the remainder of the library against serum from individuals with a particular disease of interest. Most of the work in this area has been done with peptoids (oligomers of N-alkylated glycine), which provide antibody ligands with only modest affinity and selectivity. Here, we explore the hypothesis that this is due to the 'floppiness' of the peptoid backbone by creating libraries of peptoid-like molecules that have conformation-restricting structural elements inserted into their backbones. Indeed, we show here that these libraries can provide high affinity and selectivity antigen surrogates and that this much-improved binding is completely dependent on conformational restriction of the oligomer chain.
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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.