ArticleJournal of the American Chemical Society2021
Peptoid Residues Make Diverse, Hyperstable Collagen Triple-Helices.
Article in Journal of the American Chemical Society, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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
19 citing papers in PubMed.
- Influence of linker design on the stability, folding, and assembly of tethered collagen-mimetic peptides.RSC chemical biology · 2026Article
- Structural and Positional Effects of Peptoid Residues on Triple Helix Stability.Biomacromolecules · 2026Article
- Data-Driven Engineering of Thermostable Collagen-Mimetic Peptoid Triple Helices.Macromolecular rapid communications · 2026Article
- Stereoelectronic and hydrogen-bonding effects on hydroxyproline conformation.Communications chemistry · 2026Article
- Modulating Refolding and Collagen Binding of Collagen Hybridizing Peptides through Peptoid Incorporation.Biomacromolecules · 2026Article
- Cationic Peptoids for Systemic In Vivo Cartilage-Targeting.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Around the collagen triple helix: an introduction to studying associated genetic and acquired diseases.Matrix biology : journal of the International Society for Matrix Biology · 2025Review
- Evaluation of Orientation-Dependent Cation-π Pairwise Effects within Collagen Triple Helices.The journal of physical chemistry. B · 2025Article
- Stabilization of a miniprotein fold by an unpuckered proline surrogate.Communications chemistry · 2025Article
- From Collagen Mimetics to Collagen Hybridization and Back.Accounts of chemical research · 2024Article
- Beyond N-Alkylation: Synthesis, Structure, and Function of N-Amino Peptides.Accounts of chemical research · 2024Article
- Synthesis, derivatization, and conformational scanning of peptides containing N-Aminoglycine.Methods in enzymology · 2024Article
- Bioprinting of gelatin-based materials for orthopedic application.Frontiers in bioengineering and biotechnology · 2024Review
- Cis-trans isomerization of peptoid residues in the collagen triple-helix.Nature communications · 2023Article
- Recent advances in the development of therapeutic peptides.Trends in pharmacological sciences · 2023Review
- Consequences of incorporating thiaproline and its oxidized derivatives into collagen triple helices.Protein science : a publication of the Protein Society · 2023Article
- The Chemistry and Biology of Collagen Hybridization.Journal of the American Chemical Society · 2023Review
- Collagen Molecular Damage is a Hallmark of Early Atherosclerosis Development.Journal of cardiovascular translational research · 2023Article
- Terminal repeats impact collagen triple-helix stability through hydrogen bonding.Chemical science · 2022Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
As the only ribosomally encoded N-substituted amino acid, proline promotes distinct secondary protein structures. The high proline content in collagen, the most abundant protein in the human body, is crucial to forming its hallmark structure: the triple-helix. For over five decades, proline has been considered compulsory for synthetic designs aimed at recapitulating collagen's structure and properties. Here we describe that N-substituted glycines (N-glys), also known as peptoid residues, exhibit a general triple-helical propensity similar to or greater than proline, enabling synthesis of stable triple-helical collagen mimetic peptides (CMPs) with unprecedented side chain diversity. Supported by atomic-resolution crystal structures as well as circular dichroism and computational characterizations spanning over 30 N-gly-containing CMPs, we discovered that N-glys stabilize the triple-helix primarily by sterically preorganizing individual chains into the polyproline-II helix. We demonstrated that N-glys with exotic side chains including a "click"-able alkyne and a photosensitive side chain enable CMPs for functional applications including the spatiotemporal control of cell adhesion and migration. The structural principles uncovered in this study open up opportunities for a new generation of collagen-mimetic therapeutics and materials.
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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.