ArticleChemical science2024
A high-resolution structural characterization and physicochemical study of how a peptoid binds to an oncoprotein MDM2.
Article in Chemical science, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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.
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Who cites it
3 citing papers in PubMed.
- Backbone Steric Constraints Underlie High Passive Membrane Permeability of N-Alkyl Peptides.Angewandte Chemie (International ed. in English) · 2026Article
- Uprising Unconventional Nanobiomaterials: Peptoid Nanosheets as a Multi-Modular Platform for Advanced Biological Studies.Small (Weinheim an der Bergstrasse, Germany) · 2025Review
- Solid-Phase Synthesis of Peptides with Methyl and Larger Substituents on Backbone Amide Nitrogens via On-Resin Incorporation of the Substituents.Methods in molecular biology (Clifton, N.J.) · 2025Article
Corrections and comments
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Authors and funding
13 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Peptoids are a promising drug modality targeting disease-related proteins, but how a peptoid engages in protein binding is poorly understood. This is primarily due to a lack of high-resolution peptoid-protein complex structures and systematic physicochemical studies. Here, we present the first crystal structure of a peptoid bound to a protein, providing high-resolution structural information about how a peptoid binds to a protein. We previously reported a rigid peptoid, oligo(
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Registered trials
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