ArticleNature chemistry2025
De novo design of ribosomally synthesized and post-translationally modified peptides.
Article in Nature chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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
10 citing papers in PubMed.
- A Framework for the In Vivo Production of Extensively Engineered Thiopeptides.ACS synthetic biology · 2026Article
- Repositioning the Leader Peptide in Graspetide Biosynthesis.Journal of the American Chemical Society · 2026Article
- Artificial Multidomain Ribosomally Synthesized and Post-translationally Modified Peptide Enzymes for Farnesylated Peptide Library Generation.ACS synthetic biology · 2026Article
- Leader-Independent C‑Terminal Modification by a RadicalACS bio & med chem Au · 2025Article
- Emerging strategies to enhance microbial natural product-based drug discovery.Current opinion in biotechnology · 2025Review
- LassoESM a tailored language model for enhanced lasso peptide property prediction.Nature communications · 2025Article
- Diverse thioether macrocyclized peptides through a radical SAM maturase.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Peptide and Protein Cyclization by a Promiscuous Graspetide Synthetase.ACS central science · 2025Article
- Ribosomally Synthesized and Post-Translationally Modified Peptides Assembled by ThiF-like Adenylyltransferases: Recent Advances and Future Perspectives.Molecules (Basel, Switzerland) · 2025Review
- Bacterial community in homemade kimchi and probiotic characterization ofFrontiers in microbiology · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
In nature, peptides are enzymatically modified to constrain their structure and introduce functional moieties. De novo peptide structures could be built by combining enzymes from different pathways, but determining the rules of their use is difficult. We present a biophysical model to combine enzymes sourced from bacterial ribosomally synthesized and post-translationally modified peptide (RiPP) gene clusters. Using a pipeline to evaluate more than 1,000 peptides, the model was parameterized under uniform conditions in Escherichia coli for enzymes from different classes (graspetide, spliceotide, pantocin, cyanobactin, glycocin, lasso peptide and lanthipeptide). Synthetic leader peptides with recognition sequences for up to three enzymes were designed to modify core sequences sharing no identity to natural RiPPs. Empirically, RiPPs with the desired modifications constituted 7-67% of the total peptides produced, and 6 of our 8 peptide designs were successfully modified. This work is an example of the design of enzyme-modified peptides and libraries, using a framework that can be expanded to include new enzymes and chemical moieties.
Indexed as
Identifiers
39774303What Socratic holds
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 Socratic graph.