ArticleNature communications2025
LassoESM a tailored language model for enhanced lasso peptide property prediction.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- "Lariocidin and ribosome-targeting lasso peptides as emerging antimicrobial agents against multidrug-resistant bacteria".The Journal of antibiotics · 2026Review
- Tangled Tail of Mechanically Interlocked Peptides.Journal of the American Chemical Society · 2026Review
- Precursor gene engineering expands the loop region of the lasso peptide microcin J25.RSC chemical biology · 2026Article
- Harnessing artificial intelligence for antimicrobial discovery and optimization.Current opinion in microbiology · 2026Review
- Biosynthesis, Structure, and Antibiotic Properties of Gelatinamin A, a Triculamin-Like Lasso Peptide.Chembiochem : a European journal of chemical biology · 2026Article
- Learning physical interactions to compose biological large language models.Communications chemistry · 2026Review
- Characterizing and engineering post-translational modifications with high-throughput cell-free expression.Nature communications · 2025Article
- In silico design of foldable lasso peptides.Biophysical journal · 2025Article
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Authors and funding
4 authors.
Funding
Abstract
Ribosomally synthesized and post-translationally modified peptides (RiPPs) are a diverse group of natural products. The lasso peptide class of RiPPs adopt a unique [1]rotaxane conformation formed by a lasso cyclase, conferring diverse bioactivities and remarkable stability. The prediction of lasso peptide properties, such as substrate compatibility with a particular lasso cyclase or desired biological activity, remains challenging due to limited experimental data and the complexity of substrate fitness landscapes. Here, we develop LassoESM, a tailored language model that improves lasso peptide property prediction. LassoESM embeddings enable accurate prediction of substrate compatibility, facilitate identification of novel non-cognate cyclase-substrate pairs, and enhance prediction of RNA polymerase inhibitory activity, a biological activity of several known lasso peptides. We anticipate that LassoESM and future iterations will be instrumental in the rational design and discovery of lasso peptides with tailored functions.
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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.