ArticleProtein engineering, design & selection : PEDS2011
Computational design of the lasso peptide antibiotic microcin J25.
Article in Protein engineering, design & selection : PEDS, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 21 citations in OpenAlex.
- LassoESM a tailored language model for enhanced lasso peptide property prediction.Nature communications · 2025Article
- Mutexa: A Computational Ecosystem for Intelligent Protein Engineering.Journal of chemical theory and computation · 2023Review
- How to harness biosynthetic gene clusters of lasso peptides.Journal of industrial microbiology & biotechnology · 2020Review
- Article
- Synthesis of a Peptide Derivative of MicrocinJ25 and Evaluation of Antibacterial and Biological Activities.Iranian journal of pharmaceutical research : IJPR · 2019Article
- Multispecies activity screening of microcin J25 mutants yields antimicrobials with increased specificity toward pathogenic Salmonella species relative to human commensal Escherichia coli.Biotechnology and bioengineering · 2018Article
- Free Energy Calculations of Microcin J25 Variants Binding to the FhuA Receptor.Journal of chemical theory and computation · 2017Article
- Isolation and structure determination of a new lantibiotic cinnamycin B from Actinomadura atramentaria based on genome mining.Journal of industrial microbiology & biotechnology · 2016Article
- Precursor-centric genome-mining approach for lasso peptide discovery.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
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Authors and funding
5 authors at 1 institution in 2 countries.
Funding
Abstract
Microcin J25 (MccJ25) is a 21 amino acid (aa) ribosomally synthesized antimicrobial peptide with an unusual structure in which the eight N-terminal residues form a covalently cyclized macrolactam ring through which the remaining 13 aa tail is fed. An open question is the extent of sequence space that can occupy such an extraordinary, highly constrained peptide fold. To begin answering this question, here we have undertaken a computational redesign of the MccJ25 peptide using a two-stage sequence selection procedure based on both energy minimization and fold specificity. Eight of the most highly ranked sequences from the design algorithm, each of which contained two or three amino acid substitutions, were expressed in Escherichia coli and tested for production and antimicrobial activity. Six of the eight variants were successfully produced by E.coli at production levels comparable with that of the wild-type peptide. Of these six variants, three retain detectable antimicrobial activity, although this activity is reduced relative to wild-type MccJ25. The results here build upon previous findings that even rigid, constrained structures like the lasso architecture are amenable to redesign. Furthermore, this work provides evidence that a large amount of amino acid variation is tolerated by the lasso peptide fold.
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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.