ArticleJournal of the American Chemical Society2010
Helix formation in preorganized beta/gamma-peptide foldamers: hydrogen-bond analogy to the alpha-helix without alpha-amino acid residues.
Article in Journal of the American Chemical Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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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
11 citing papers in PubMed.
- Tackling Undruggable Targets with Designer Peptidomimetics and Synthetic Biologics.Chemical reviews · 2024Review
- Foldamers controlled by functional triamino acids: structural investigation of α/γ-hybrid oligopeptides.Communications chemistry · 2024Article
- Unnatural helical peptidic foldamers as protein segment mimics.Chemical Society reviews · 2023Review
- Environmental Modulation of Chiral Prolinamide Catalysts for Stereodivergent Conjugate Addition.Journal of catalysis · 2022Article
- α,ε-Hybrid Peptide Foldamers: Self-Assembly of Peptide with Trans Carbon-Carbon Double Bonds in the Backbone and Its Saturated Analogue.ACS omega · 2018Article
- Impact of γ-Amino Acid Residue Preorganization on α/γ-Peptide Foldamer Helicity in Aqueous Solution.Journal of the American Chemical Society · 2016Article
- Heterogeneous H-bonding in a foldamer helix.Journal of the American Chemical Society · 2015Article
- 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
- New preorganized γ-amino acids as foldamer building blocks.Organic letters · 2012Article
- Structural mimicry of the α-helix in aqueous solution with an isoatomic α/β/γ-peptide backbone.Journal of the American Chemical Society · 2011Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
We report the first high-resolution structural data for the beta/gamma-peptide 13-helix (i,i+3 C=O...H-N H-bonds), a secondary structure that is formed by oligomers with a 1:1 alternation of beta- and gamma-amino acid residues. Our characterization includes both crystallographic and 2D NMR data. Previous studies suggested that beta/gamma-peptides constructed from conformationally flexible residues adopt a different helical secondary structure in solution. Our design features preorganized beta- and gamma-residues, which strongly promote 13-helical folding by the 1:1 beta/gamma backbone.
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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.