{
  "abstract": "Lipopeptides possess diverse bioactivities with widespread uses as antimicrobial drugs and biosurfactants but their biosynthetic engineering remains challenging. Classical lipopeptides (such as daptomycin or surfactin) are biosynthesized by modular, non-ribosomal megasynthetases. An alternative streamlined route to lipopeptides are the ribosomally synthesized and post-translationally modified peptides (RiPPs) derived from gene-encoded precursor proteins. We recently characterized a novel class of post-translational modification enzymes in RiPPs that catalyze fatty acylation of ornithine and lysine side chains. The resulting lipopeptides were termed selidamides. To assess the use of selidamide N-acyltransferases as biocatalysts, we probed the peptide substrate specificity of the model lauroyl-transferase KspN from kamptornamide biosynthesis. Nearest-neighbor, lysine-scan, and truncation mutants demonstrated promiscuity for the peptide substrate. As a proof-of-concept toward designer lipopeptides using RiPP biosynthetic principles, we produced sequences mimicking bioactive non-ribosomal lipopeptides and tested their conversion by maturases from the kamptornamide biosynthetic pathway. Ornithines, fatty acyl groups, and lanthionine macrocycles were installed in the mimics as a promising start toward the directed biosynthesis of custom lipopeptides.",
  "abstract_shown": true,
  "affiliations": [
    "Institute of Microbiology, Eidgenössische Technische Hochschule (ETH) Zürich, Vladimir-Prelog-Weg 4 8093 Zürich Switzerland"
  ],
  "article_type": "research article",
  "arxiv": null,
  "author_total": 9,
  "authors": [
    {
      "affs": [
        0
      ],
      "name": "Nina M. Bösch",
      "orcid": "0000-0001-6656-7040"
    },
    {
      "affs": [
        0
      ],
      "name": "Manon Coste",
      "orcid": "0009-0008-3881-7856"
    },
    {
      "affs": [
        0
      ],
      "name": "Johannes A. Rudmann Eckert",
      "orcid": "0000-0002-5398-0562"
    },
    {
      "affs": [
        0
      ],
      "name": "Gabriel Cervera Arriaga",
      "orcid": "0009-0002-0415-5299"
    },
    {
      "affs": [
        0
      ],
      "name": "Annina R. Meyer",
      "orcid": "0009-0006-3110-6598"
    },
    {
      "affs": [
        0
      ],
      "name": "Eléonore Moore",
      "orcid": "0009-0009-8359-6447"
    },
    {
      "affs": [
        0
      ],
      "name": "Daniel Richter",
      "orcid": "0000-0003-2583-520X"
    },
    {
      "affs": [
        0
      ],
      "name": "Jörn Piel",
      "orcid": "0000-0002-2282-8154"
    },
    {
      "affs": [
        0
      ],
      "name": "Anna L. Vagstad",
      "orcid": "0000-0001-8074-0137"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/f168194drbe8a.bib",
  "cited_by": 0,
  "doi": "10.1039/d6cb00169f",
  "fulltext_url": "https://pmc.ncbi.nlm.nih.gov/articles/PMC13647313/",
  "id": "f168194drbe8a",
  "issns": [
    "2633-0679"
  ],
  "landing_url": "https://doi.org/10.1039/d6cb00169f",
  "language": "en",
  "licence": "CC-BY-NC-3.0",
  "licence_label": "CC BY-NC 3.0",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by-nc/3.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "heading",
      "Chemistry"
    ],
    [
      "openalex",
      "2402|Microbial Natural Products and Biosynthesis"
    ]
  ],
  "openalex": "W7220660428",
  "pdf_url": null,
  "pmcid": "PMC13647313",
  "pmid": "42851787",
  "published": "2026-10-06",
  "publisher": "Royal Society of Chemistry",
  "ris": "https://research.draconitic.com/paper/f168194drbe8a.ris",
  "sources": [
    {
      "first_seen": "2026-11-07T12:23:31Z",
      "native_id": "PMC13647313",
      "source": "pmc",
      "url": "https://doi.org/10.1039/d6cb00169f"
    }
  ],
  "subjects": [
    {
      "field": "biology",
      "origin": "openalex:2402|Microbial Natural Products and Biosynthesis",
      "subfield": "microbiology"
    }
  ],
  "title": "Exploring RiPP-derived N-acyltransferases for genetically encoded lipopeptide engineering",
  "title_text": "Exploring RiPP-derived N-acyltransferases for genetically encoded lipopeptide engineering",
  "type": "peer-reviewed",
  "updated_at": "2026-11-08T12:21:00Z",
  "url": "https://research.draconitic.com/paper/f168194drbe8a",
  "venue": "RSC Chemical Biology",
  "versions": []
}