ArticleAngewandte Chemie (International ed. in English)2018
De Novo Left-Handed Synthetic Peptidomimetic Foldamers.
Article in Angewandte Chemie (International ed. in English), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed.
- α/Sulfonyl-γ-AApeptide foldamers mitigate Alzheimer's disease pathology by stabilizing transient helical domains in Aβ.Nature communications · 2026Article
- Discovery of peptidomimetic inhibitors of CREB/CBP by targeting hydrophobic grooves on the surface of the CBP KIX domain.Acta pharmaceutica Sinica. B · 2025Article
- Recognition of the CREB-Binding Protein/Mixed Lineage Leukemia Interface by Sulfonyl-γ-AApeptides: Beyond Mimicry of Mixed Lineage Leukemia.Journal of medicinal chemistry · 2025Article
- Structure and Function of the SARS-CoV-2 6-HB Fusion Core and Peptide-based Fusion Inhibitors: A Review.Current medicinal chemistry · 2025Review
- Tackling Undruggable Targets with Designer Peptidomimetics and Synthetic Biologics.Chemical reviews · 2024Review
- Helical sulfonyl-γ-AApeptides for the inhibition of HIV-1 fusion and HIF-1α signaling.RSC medicinal chemistry · 2024Review
- Helical sulfonyl-γ-AApeptides modulating Aβ oligomerization and cytotoxicity by recognizing Aβ helix.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Ambidexterity and Left-Handedness Induced by Geminally Disubstituted γ Amino Acid Residues in Chiral 3ACS omega · 2023Article
- Inhibition of Hypoxia-Inducible Transcription Factor (HIF-1α) Signaling with Sulfonyl-γ-AApeptide Helices.Journal of the American Chemical Society · 2023Article
- Unnatural helical peptidic foldamers as protein segment mimics.Chemical Society reviews · 2023Review
- Structure-Based Design of Peptides Targeting VEGF/VEGFRs.Pharmaceuticals (Basel, Switzerland) · 2023Review
- An HR2-Mimicking Sulfonyl-γ-AApeptide Is a Potent Pan-coronavirus Fusion Inhibitor with Strong Blood-Brain Barrier Permeability, Long Half-Life, and Promising Oral Bioavailability.ACS central science · 2023Article
- Sulfono-γ-AApeptides as Protein Helical Domain Mimetics to Manipulate the Angiogenesis.Chembiochem : a European journal of chemical biology · 2022Article
- Determination of the critical chain length for macromolecular crystallization using structurally flexible polyketones.Chemical science · 2022Article
- Helical sulfono-γ-AApeptides with predictable functions in protein recognition.RSC chemical biology · 2022Review
- Using proteomimetics to switch angiogenic signaling.Acta pharmaceutica Sinica. B · 2022Article
- Activation of E6AP/UBE3A-Mediated Protein Ubiquitination and Degradation Pathways by a Cyclic γ-AA Peptide.Journal of medicinal chemistry · 2022Article
- Modulating Angiogenesis by Proteomimetics of Vascular Endothelial Growth Factor.Journal of the American Chemical Society · 2022Article
- α/Sulfono-γ-AApeptide Hybrid Analogues of Glucagon with Enhanced Stability and Prolonged In Vivo Activity.Journal of medicinal chemistry · 2021Article
- Peptidomimetic-based antibody surrogate for HER2.Acta pharmaceutica Sinica. B · 2021Article
Corrections and comments
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Authors and funding
11 authors.
Funding
Abstract
The development of peptidomimetic helical foldamers with a wide repertoire of functions is of significant interest. Herein, we report the X-ray crystal structures of a series of homogeneous l-sulfono-γ-AA foldamers and elucidate their folding conformation at the atomic level. Single-crystal X-ray crystallography revealed that this class of oligomers fold into unprecedented dragon-boat-shaped and unexpected left-handed helices, which are stabilized by the 14-hydrogen-bonding pattern present in all sequences. These l-sulfono-γ-AApeptides have a helical pitch of 5.1 Å and exactly four side chains per turn, and the side chains lie perfectly on top of each other along the helical axis. 2D NMR spectroscopy, computational simulations, and CD studies support the folding conformation in solution. Our results provide a structural basis at the atomic level for the design of novel biomimetics with a precise arrangement of functional groups in three dimensions.
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