ArticleJournal of the American Chemical Society2015
Disulfide-Mediated β-Strand Dimers: Hyperstable β-Sheets Lacking Tertiary Interactions and Turns.
Article in Journal of the American Chemical Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Design Principles for β-Solenoid Stability via Covalent and Electrostatic Capping Motifs.The journal of physical chemistry letters · 2026Article
- Cryostorage-induced water dynamics in whole egg liquid gels: macrostructural transformations and molecular dehydration mechanisms.Food chemistry: X · 2026Article
- Intrastrand Peptide Staples That Promote β-Sheet Folding, Self-Assembly, and Amyloid Seeding.Journal of the American Chemical Society · 2025Article
- From Concepts to Inhibitors: A Blueprint for Targeting Protein-Protein Interactions.Chemical reviews · 2025Review
- Macrocyclic β-Sheets Stabilized by Hydrogen Bond Surrogates.Angewandte Chemie (International ed. in English) · 2023Article
- Bicyclic β-Sheet Mimetics that Target the Transcriptional Coactivator β-Catenin and Inhibit Wnt Signaling.Angewandte Chemie (International ed. in English) · 2021Article
- Bent Into Shape: Folded Peptides to Mimic Protein Structure and Modulate Protein Function.Peptide science (Hoboken, N.J.) · 2020Article
- Protein stabilization by tuning the steric restraint at the reverse turn.Chemical science · 2018Article
- Toward a Soluble Model System for the Amyloid State.Journal of the American Chemical Society · 2017Article
- Cyclic oligomer design with de novo αβ-proteins.Protein science : a publication of the Protein Society · 2017Article
- Hairpin structure stability plays a role in the activity of two antimicrobial peptides.FEBS letters · 2016Article
- Lasso Peptide Biosynthetic Protein LarB1 Binds Both Leader and Core Peptide Regions of the Precursor Protein LarA.ACS central science · 2016Article
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Authors and funding
3 authors.
Funding
Abstract
Disulfide bonds between cysteine residues are essential to the structure and folding of many proteins. Yet their role in the design of structured peptides and proteins has frequently been limited to use as intrachain covalent staples that reinforce existing structure or induce knot-like conformations. In β-hairpins, their placement at non-H-bonding positions across antiparallel strands has proven useful for achieving fully folded positive controls. Here we report a new class of designed β-sheet peptide dimers with strand-central disulfides as a key element. We have found that the mere presence of a disulfide bond near the middle of a short peptide chain is sufficient to nucleate some antiparallel β-sheet structure; addition of β-capping units and other favorable cross-strand interactions yield hyperstable sheets. Strand-central cystines were found to be superior to the best designed reversing turns in terms of nucleating β-sheet structure formation. We have explored the limitations and possibilities of this technique (the use of disulfides as sheet nucleators), and we provide a set of rules and rationales for the application and further design of disulfide-tethered "turnless" β-sheets.
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