ArticleNature communications2020
Ribosome-mediated polymerization of long chain carbon and cyclic amino acids into peptides in vitro.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 90 citations in OpenAlex.
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- Aminoacyl-tRNA Specificity of a Ligase Catalyzing Non-ribosomal Peptide Extension.Journal of the American Chemical Society · 2025Article
- Site-selective protein editing by backbone extension acyl rearrangements.Nature chemical biology · 2025Article
- Cell-Free Gene Expression: Methods and Applications.Chemical reviews · 2025Review
- Cell-Free Systems: Ideal Platforms for Accelerating the Discovery and Production of Peptide-Based Antibiotics.International journal of molecular sciences · 2024Review
- A Translation-Independent Directed Evolution Strategy to Engineer Aminoacyl-tRNA Synthetases.ACS central science · 2024Article
- Engineering tRNAs for the Ribosomal Translation of Non-proteinogenic Monomers.Chemical reviews · 2024Review
- Cheminformatics-Guided Cell-Free Exploration of Peptide Natural Products.Journal of the American Chemical Society · 2024Article
- Engineered mRNA-ribosome fusions for facile biosynthesis of selenoproteins.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Tuning tRNAs for improved translation.Frontiers in genetics · 2024Review
- Article
- Atomistic simulations of the Escherichia coli ribosome provide selection criteria for translationally active substrates.Nature chemistry · 2023Article
- In vitro selection of macrocyclic peptide inhibitors containing cyclic γNature chemistry · 2023Article
- Expanding the substrate scope of pyrrolysyl-transfer RNA synthetase enzymes to include non-α-amino acids in vitro and in vivo.Nature chemistry · 2023Article
- Aminobenzoic Acid Derivatives Obstruct Induced Fit in the Catalytic Center of the Ribosome.ACS central science · 2023Article
- Mapping the in vivo fitness landscape of a tethered ribosome.Science advances · 2023Article
- The SARS-CoV-2 Hydra, a tiny monster from the 21st century: Thermodynamics of the BA.5.2 and BF.7 variants.Microbial risk analysis · 2023Article
- Never ending story? Evolution of SARS-CoV-2 monitored through Gibbs energies of biosynthesis and antigen-receptor binding of Omicron BQ.1, BQ.1.1, XBB and XBB.1 variants.Microbial risk analysis · 2023Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ribosome-mediated polymerization of backbone-extended monomers into polypeptides is challenging due to their poor compatibility with the translation apparatus, which evolved to use α-L-amino acids. Moreover, mechanisms to acylate (or charge) these monomers to transfer RNAs (tRNAs) to make aminoacyl-tRNA substrates is a bottleneck. Here, we rationally design non-canonical amino acid analogs with extended carbon chains (γ-, δ-, ε-, and ζ-) or cyclic structures (cyclobutane, cyclopentane, and cyclohexane) to improve tRNA charging. We then demonstrate site-specific incorporation of these non-canonical, backbone-extended monomers at the N- and C- terminus of peptides using wild-type and engineered ribosomes. This work expands the scope of ribosome-mediated polymerization, setting the stage for new medicines and materials.
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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.