Natural Product-Derived Ianthelliformisamines Inhibit Protein Translation and Block Bacterial Flagellum Assembly
into human host cells. This work illustrates how activity-based chemical proteomics can uncover previously unrecognized cellular targets for natural product scaffolds, thereby revealing distinct modes of action and supporting further therapeutic development.
Authors
- Daniel N. Wilson (ORCID: https://orcid.org/0000-0003-3816-3828)
- Michael Isselstein
- Martino Morici (ORCID: https://orcid.org/0000-0002-7304-5264)
- Sophie Brameyer (ORCID: https://orcid.org/0000-0002-6779-2343)
- Stephan A. Sieber (ORCID: https://orcid.org/0000-0002-9400-906X)
- Max Bottlinger
- Elena Fajardo-Ruiz (ORCID: https://orcid.org/0000-0002-0421-9558)
- Max Berger
- Kirsten Jung
- Isabella Gantner
Institutions
- University of Copenhagen (DK)
- Universität Hamburg (DE)
- Faculty (United Kingdom) (GB)
- Microbiology Society (GB)
- Czech Academy of Sciences, Institute of Microbiology (CZ)
- Geophysical Laboratory (US)
- Austrian Centre for Electron Microscopy and Nanoanalysis (AT)
- Technical University of Munich (DE)
- Ludwig-Maximilians-Universität München (DE)
Publication Details
- Journal
- ACS Chemical Biology
- Published
- 2026-04-21
- DOI
- https://doi.org/10.1021/acschembio.5c01018
- Primary Topic
- Biochemical and Structural Characterization
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- Merck KGaA
- Deutsche Forschungsgemeinschaft