ArticleACS chemical biology2018
Hydrogen Bond Surrogate Stabilization of β-Hairpins.
Article in ACS chemical biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 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
24 citing papers in PubMed, 38 citations in OpenAlex.
- MinimalRSC chemical biology · 2026Article
- Cyclic Peptides as Modulators of Protein-Protein Interactions: A Survival Guide from Discovery Platforms to AI-Driven Design.International journal of molecular sciences · 2026Review
- Backbone double-mutant cycle analysis quantifies hydrogen-bond energies in proteins.Protein science : a publication of the Protein Society · 2026Article
- From Concepts to Inhibitors: A Blueprint for Targeting Protein-Protein Interactions.Chemical reviews · 2025Review
- β-Hairpin Peptidomimetics for Protein-Protein Interaction Inhibition.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Tackling Undruggable Targets with Designer Peptidomimetics and Synthetic Biologics.Chemical reviews · 2024Review
- Selection of Nucleotide-Encoded Mass Libraries of Macrocyclic Peptides for Inaccessible Drug Targets.Chemical reviews · 2024Review
- Structural Characterization of Disulfide-Linked p53-Derived Peptide Dimers.Research square · 2024Article
- Structure and biological activity in vitro of Flagellin and its mutants from Escherichia coli Nissle 1917.Archives of microbiology · 2024Article
- Stabilized cyclic peptides as modulators of protein-protein interactions: promising strategies and biological evaluation.RSC medicinal chemistry · 2023Review
- Macrocyclic β-Sheets Stabilized by Hydrogen Bond Surrogates.Angewandte Chemie (International ed. in English) · 2023Article
- Structure-Based Design and Synthesis of StapledJournal of medicinal chemistry · 2023Article
- Stapled β-Hairpin Antimicrobial Peptides with Improved Stability and Activity against Drug-Resistant Gram-Negative Bacteria.Journal of medicinal chemistry · 2023Article
- The Composition, Structure, and Functionalities of Prolamins from Highland Barley.Molecules (Basel, Switzerland) · 2023Article
- Hopping or Tunneling? Tailoring the Electron Transport Mechanisms through Hydrogen Bonding Geometry in the Boron-Doped Diamond Molecular Junctions.The journal of physical chemistry letters · 2022Article
- Structure-Based Design of Stapled Peptides That Bind GABARAP and Inhibit Autophagy.Journal of the American Chemical Society · 2022Article
- Structural basis for inhibition of the drug efflux pump NorA from Staphylococcus aureus.Nature chemical biology · 2022Article
- Therapeutic peptides: current applications and future directions.Signal transduction and targeted therapy · 2022Review
- Chiral, sequence-definable foldamer-derived macrocycles.Chemical science · 2021Article
- Folding in Place: Design of β-Strap Motifs to Stabilize the Folding of Hairpins with Long Loops.The Journal of organic chemistry · 2021Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Peptide secondary and tertiary structure motifs frequently serve as inspiration for the development of protein-protein interaction (PPI) inhibitors. While a wide variety of strategies have been used to stabilize or imitate α-helices, similar strategies for β-sheet stabilization are more limited. Synthetic scaffolds that stabilize reverse turns and cross-strand interactions have provided important insights into β-sheet stability and folding. However, these templates occupy regions of the β-sheet that might impact the β-sheet's ability to bind at a PPI interface. Here, we present the hydrogen bond surrogate (HBS) approach for stabilization of β-hairpin peptides. The HBS linkage replaces a cross-strand hydrogen bond with a covalent linkage, conferring significant conformational and proteolytic resistance. Importantly, this approach introduces the stabilizing linkage in the buried β-sheet interior, retains all side chains for further functionalization, and allows efficient solid-phase macrocyclization. We anticipate that HBS stabilization of PPI β-sheets will enhance the development of β-sheet PPI inhibitors and expand the repertoire of druggable PPIs.
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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.