ArticleNature chemistry2018
Ribosomal synthesis and folding of peptide-helical aromatic foldamer hybrids.
Article in Nature chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 37 papers, 1 of them a synthesis that pooled it.
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Who cites it
37 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Cell-Free Approach for Non-canonical Amino Acids Incorporation Into Polypeptides.Frontiers in bioengineering and biotechnology · 2020Pooled it
- Quinoline-Directed Folding in Anilide-Quinoline Hybrids: Length-Controlled Three-Dimensional Conformational Diversity.JACS Au · 2026Article
- A glycan foldamer that uses carbohydrate-aromatic interactions to perform catalysis.Nature chemistry · 2025Article
- Reprogramming the genetic code with flexizymes.Nature reviews. Chemistry · 2024Review
- Breaking the Degeneracy of Sense Codons - How Far Can We Go?Israel journal of chemistry · 2024Article
- Application of artificial backbone connectivity in the development of metalloenzyme mimics.Current opinion in chemical biology · 2024Review
- Engineering tRNAs for the Ribosomal Translation of Non-proteinogenic Monomers.Chemical reviews · 2024Review
- Tuning tRNAs for improved translation.Frontiers in genetics · 2024Review
- Harnessing Aromatic-Histidine Interactions through Synergistic Backbone Extension and Side Chain Modification.Angewandte Chemie (International ed. in English) · 2023Article
- Evaluating Translational Efficiency of Noncanonical Amino Acids to Inform the Design of Druglike Peptide Libraries.ACS chemical biology · 2023Article
- Differential Peptide Multi-Macrocyclizations at the Surface of a Helical Foldamer Template.Angewandte Chemie (International ed. in English) · 2022Article
- Mobile Translation Systems Generate Genomically EngineeredACS synthetic biology · 2022Article
- Chiral, sequence-definable foldamer-derived macrocycles.Chemical science · 2021Article
- Directed Evolution in Drops: Molecular Aspects and Applications.ACS synthetic biology · 2021Review
- Conformational interplay in hybrid peptide-helical aromatic foldamer macrocycles.Chemical science · 2021Article
- A versatile living polymerization method for aromatic amides.Nature chemistry · 2021Article
- Strategies to expand peptide functionality through hybridisation with a small molecule component.RSC chemical biology · 2021Review
- Article
- Mechanistic studies of non-canonical amino acid mutagenesis.Methods in enzymology · 2021Article
- Initiating protein synthesis with noncanonical monomers in vitro and in vivo.Methods in enzymology · 2021Article
Corrections and comments
- Erratum issued
Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Translation, the mRNA-templated synthesis of peptides by the ribosome, can be manipulated to incorporate variants of the 20 cognate amino acids. Such approaches for expanding the range of chemical entities that can be produced by the ribosome may accelerate the discovery of molecules that can perform functions for which poorly folded, short peptidic sequences are ill suited. Here, we show that the ribosome tolerates some artificial helical aromatic oligomers, so-called foldamers. Using a flexible tRNA-acylation ribozyme-flexizyme-foldamers were attached to tRNA, and the resulting acylated tRNAs were delivered to the ribosome to initiate the synthesis of non-cyclic and cyclic foldamer-peptide hybrid molecules. Passing through the ribosome exit tunnel requires the foldamers to unfold. Yet foldamers encode sufficient folding information to influence the peptide structure once translation is completed. We also show that in cyclic hybrids, the foldamer portion can fold into a helix and force the peptide segment to adopt a constrained and stretched conformation.
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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.