ArticleJournal of the American Chemical Society2017
Right-Handed Helical Foldamers Consisting of De Novo d-AApeptides.
Article in Journal of the American Chemical Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- 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
- Unnatural helical peptidic foldamers as protein segment mimics.Chemical Society reviews · 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
- Article
- Sulfono-γ-AApeptides as Protein Helical Domain Mimetics to Manipulate the Angiogenesis.Chembiochem : a European journal of chemical biology · 2022Article
- Helical sulfono-γ-AApeptides with predictable functions in protein recognition.RSC chemical biology · 2022Review
- Peptidomimetic-based antibody surrogate for HER2.Acta pharmaceutica Sinica. B · 2021Article
- Potential Foldamers Based on anOrganic letters · 2021Article
- The folding propensity of α/sulfono-γ-AA peptidic foldamers with both left- and right-handedness.Communications chemistry · 2021Article
- Rational Design of Right-Handed Heterogeneous Peptidomimetics as Inhibitors of Protein-Protein Interactions.Journal of medicinal chemistry · 2020Article
- Sulfono-γ-AApeptides as Helical Mimetics: Crystal Structures and Applications.Accounts of chemical research · 2020Article
- Rational Design and Synthesis of Right-Handed d-Sulfono-γ-AApeptide Helical Foldamers as Potent Inhibitors of Protein-Protein Interactions.The Journal of organic chemistry · 2020Article
- Stereoselective and Divergent Construction of β-Thiolated/Selenolated Amino Acids via Photoredox-Catalyzed Asymmetric Giese Reaction.Journal of the American Chemical Society · 2020Article
- Aggregation-Induced Emissive and Circularly Polarized Homogeneous Sulfono-γ-AApeptide Foldamers.Advanced optical materials · 2020Article
- α-Helix-Mimicking Sulfono-γ-AApeptide Inhibitors for p53-MDM2/MDMX Protein-Protein Interactions.Journal of medicinal chemistry · 2020Article
- γ-AApeptides-based Small Molecule Ligands That Disaggregate Human Islet Amyloid Polypeptide.Scientific reports · 2020Article
- Dimeric γ-AApeptides With Potent and Selective Antibacterial Activity.Frontiers in chemistry · 2020Article
- Helical Sulfono-γ-AApeptides with Aggregation-Induced Emission and Circularly Polarized Luminescence.Journal of the American Chemical Society · 2019Article
- Orthogonal Halogen-Bonding-Driven 3D Supramolecular Assembly of Right-Handed Synthetic Helical Peptides.Angewandte Chemie (International ed. in English) · 2019Article
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Authors and funding
11 authors.
Funding
Abstract
New types of foldamer scaffolds are formidably challenging to design and synthesize, yet highly desirable as structural mimics of peptides/proteins with a wide repertoire of functions. In particular, the development of peptidomimetic helical foldamers holds promise for new biomaterials, catalysts, and drug molecules. Unnatural l-sulfono-γ-AApeptides were recently developed and shown to have potential applications in both biomedical and material sciences. However, d-sulfono-γ-AApeptides, the enantiomers of l-sulfono-γ-AApeptides, have never been studied due to the lack of high-resolution three-dimensional structures to guide structure-based design. Herein, we report the first synthesis and X-ray crystal structures of a series of 2:1 l-amino acid/d-sulfono-γ-AApeptide hybrid foldamers, and elucidate their folded conformation at the atomic level. Single-crystal X-ray crystallography indicates that this class of oligomers folds into well-defined right-handed helices with unique helical parameters. The helical structures were consistent with data obtained from solution 2D NMR, CD studies, and molecular dynamics simulations. Our findings are expected to inspire the structure-based design of this type of unique folding biopolymers for biomaterials and biomedical applications.
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