ArticleJournal of the American Chemical Society2011
Structural mimicry of the α-helix in aqueous solution with an isoatomic α/β/γ-peptide backbone.
Article in Journal of the American Chemical Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Tackling Undruggable Targets with Designer Peptidomimetics and Synthetic Biologics.Chemical reviews · 2024Review
- In Vitro Selection of Macrocyclic l-α/d-α/β/γ-Hybrid Peptides Targeting IFN-γ/IFNGR1 Protein-Protein Interaction.Journal of the American Chemical Society · 2024Article
- Foldamers controlled by functional triamino acids: structural investigation of α/γ-hybrid oligopeptides.Communications chemistry · 2024Article
- Hormone Analogues with Unique Signaling Profiles from Replacement of α-Residue Triads with β/γ Diads.Journal of the American Chemical Society · 2023Article
- The folding propensity of α/sulfono-γ-AA peptidic foldamers with both left- and right-handedness.Communications chemistry · 2021Article
- Aromatic Foldamer Helices as α-Helix Extended Surface Mimetics.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020Article
- Differential Effects of βAngewandte Chemie (International ed. in English) · 2018Article
- Impact of Backbone Pattern and Residue Substitution on Helicity in α/β/γ-Peptides.Journal of the American Chemical Society · 2018Article
- An α-Helix-Mimicking 12,13-Helix: Designed α/β/γ-Foldamers as Selective Inhibitors of Protein-Protein Interactions.Angewandte Chemie (International ed. in English) · 2016Article
- Impact of γ-Amino Acid Residue Preorganization on α/γ-Peptide Foldamer Helicity in Aqueous Solution.Journal of the American Chemical Society · 2016Article
- Systematic Targeting of Protein-Protein Interactions.Trends in pharmacological sciences · 2016Review
- Evaluation of a cyclopentane-based γ-amino acid for the ability to promote α/γ-peptide secondary structure.The Journal of organic chemistry · 2013Article
- Differential impact of β and γ residue preorganization on α/β/γ-peptide helix stability in water.Journal of the American Chemical Society · 2013Article
- Inhibition of α-helix-mediated protein-protein interactions using designed molecules.Nature chemistry · 2013Review
- α-Helix mimicry with α/β-peptides.Methods in enzymology · 2013Article
- Nucleation effects in peptide foldamers.Journal of the American Chemical Society · 2012Article
- New preorganized γ-amino acids as foldamer building blocks.Organic letters · 2012Article
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Authors and funding
2 authors.
Funding
Abstract
Artificial mimicry of α-helices offers a basis for development of protein-protein interaction antagonists. Here we report a new type of unnatural peptidic backbone, containing α-, β-, and γ-amino acid residues in an αγααβα repeat pattern, for this purpose. This unnatural hexad has the same number of backbone atoms as a heptad of α residues. Two-dimensional NMR data clearly establish the formation of an α-helix-like conformation in aqueous solution. The helix formed by our 12-mer α/β/γ-peptide is considerably more stable than the α-helix formed by an analogous 14-mer α-peptide, presumably because of the preorganized β and γ residues employed.
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Registered trials
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