ArticleChembiochem : a European journal of chemical biology2018
Design of a Short Thermally Stable α-Helix Embedded in a Macrocycle.
Article in Chembiochem : a European journal of chemical biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Dual-Capped Helical Interface Mimics.Journal of the American Chemical Society · 2024Article
- Bicyclic Schellman Loop Mimics (BSMs): Rigid SyntheticACS central science · 2023Article
- Unprotected peptide macrocyclization and stapling via a fluorine-thiol displacement reaction.Nature communications · 2022Article
- Design and synthesis of Nrf2-derived hydrocarbon stapled peptides for the disruption of protein-DNA-interactions.PloS one · 2022Article
- Folding-controlled assembly ofChemical science · 2021Article
- N-locking stabilization of covalent helical peptides: Application to Bfl-1 antagonists.Chemical biology & drug design · 2020Article
- Modulation of Coiled-Coil Binding Strength and Fusogenicity through Peptide Stapling.Bioconjugate chemistry · 2020Article
- Macrocycles of higherChemical science · 2019Article
- Recent structural advances in constrained helical peptides.Medicinal research reviews · 2019Review
- Exposing the Nucleation Site in α-Helix Folding: A Joint Experimental and Simulation Study.The journal of physical chemistry. B · 2019Article
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Authors and funding
7 authors.
Funding
Abstract
Although helices play key roles in peptide-protein and protein-protein interactions, the helical conformation is generally unstable for short peptides (10-15 residues) in aqueous solution in the absence of their binding partners. Thus, stabilizing the helical conformation of peptides can lead to increases in binding potency, specificity, and stability towards proteolytic degradation. Helices have been successfully stabilized by introducing side chain-to-side chain crosslinks within the central portion of the helix. However, this approach leaves the ends of the helix free, thus leading to fraying and exposure of the non-hydrogen-bonded amide groups to solvent. Here, we develop a "capped-strapped" peptide strategy to stabilize helices by embedding the entire length of the helix within a macrocycle, which also includes a semirigid organic template as well as end-capping interactions. We have designed a ten-residue capped-strapped helical peptide that behaves like a miniprotein, with a cooperative thermal unfolding transition and T
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