ArticleNature chemical biology2025
Substrate interactions guide cyclase engineering and lasso peptide diversification.
Article in Nature chemical biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Synthesis of β-Thiolated Amino Acids: Investigation Toward the Total Chemical Synthesis of Lasso Peptide Microcin J25.Chembiochem : a European journal of chemical biology · 2026Article
- Precursor gene engineering expands the loop region of the lasso peptide microcin J25.RSC chemical biology · 2026Article
- Tangled Tail of Mechanically Interlocked Peptides.Journal of the American Chemical Society · 2026Review
- Biosynthesis, Structure, and Antibiotic Properties of Gelatinamin A, a Triculamin-Like Lasso Peptide.Chembiochem : a European journal of chemical biology · 2026Article
- De novo Folding Mechanisms of Lasso Peptides.bioRxiv : the preprint server for biology · 2026Article
- A Versatile Enzymatic Pathway for Modification of Peptide C‑Termini.ACS central science · 2025Article
- LassoESM a tailored language model for enhanced lasso peptide property prediction.Nature communications · 2025Article
- Lasso Peptides-A New Weapon Against Superbugs.International journal of molecular sciences · 2025Review
- Advances in Peptidomimetics for Next-Generation Therapeutics: Strategies, Modifications, and Applications.Chemical reviews · 2025Review
- Evolution-Guided Discovery of Antimycobacterial Triculamin-Like Lasso Peptides.Angewandte Chemie (International ed. in English) · 2025Article
- In silico design of foldable lasso peptides.Biophysical journal · 2025Article
- Substrate recognition by a peptide-aminoacyl-tRNA ligase.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
Corrections and comments
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Authors and funding
14 authors.
Funding
Abstract
Lasso peptides are a diverse class of naturally occurring, highly stable molecules kinetically trapped in a distinctive [1]rotaxane conformation. How the ATP-dependent lasso cyclase constrains a relatively unstructured substrate peptide into a low entropy product has remained a mystery owing to poor enzyme stability and activity in vitro. In this study, we combined substrate tolerance data with structural predictions, bioinformatic analysis, molecular dynamics simulations and mutational scanning to construct a model for the three-dimensional orientation of the substrate peptide in the lasso cyclase active site. Predicted peptide cyclase molecular contacts were validated by rationally engineering multiple, phylogenetically diverse lasso cyclases to accept substrates rejected by the wild-type enzymes. Finally, we demonstrate the utility of lasso cyclase engineering by robustly producing previously inaccessible variants that tightly bind to integrin αvβ8, which is a primary activator of transforming growth factor β and, thus, an important anti-cancer target.
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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.