Identification of Antibacterial Cyclic Peptides with a High-Throughput Cell-Based Dropout Screen

Antimicrobial resistance is a growing global health threat, necessitating new antibiotics and discovery strategies. Here, we report a target-agnostic negative-selection screening platform that combines an intracellular library of 3.2 million cyclic peptides with next-generation sequencing to identify antibacterial cyclic peptides through the depletion of their encoding sequences. Clustering of depleted sequences by shared pharmacophores enables robust hit identification and allows focused library design. Using this approach, we identify a cyclic peptide scaffold that inhibits the previously untargeted essential iron-sulfur cluster carrier protein ErpA. This work establishes a general and scalable framework for the discovery of intracellular antibacterial targets and associated inhibitors directly in living cells.

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Publication Details

Journal
Journal of the American Chemical Society
Published
2026-07-26
DOI
https://doi.org/10.1021/jacs.6c09188
Primary Topic
Chemical Synthesis and Analysis
Type
article
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article

Identification of Antibacterial Cyclic Peptides with a High-Throughput Cell-Based Dropout Screen

Leonie M. Windeln, Ali Tavassoli, Abbas M. Walji, Alexander McDermott et al.
Journal of the American Chemical Society
Chemical Synthesis and Analysis
article

Identification of Antibacterial Cyclic Peptides with a High-Throughput Cell-Based Dropout Screen

Leonie M. Windeln, Ali Tavassoli, Abbas M. Walji, Alexander McDermott, Agnieszka B. Wisniewska, Lewis W. Mitchell, Scott S. Walker
article en

Abstract

Antimicrobial resistance is a growing global health threat, necessitating new antibiotics and discovery strategies. Here, we report a target-agnostic negative-selection screening platform that combines an intracellular library of 3.2 million cyclic peptides with next-generation sequencing to identify antibacterial cyclic peptides through the depletion of their encoding sequences. Clustering of depleted sequences by shared pharmacophores enables robust hit identification and allows focused library design. Using this approach, we identify a cyclic peptide scaffold that inhibits the previously untargeted essential iron-sulfur cluster carrier protein ErpA. This work establishes a general and scalable framework for the discovery of intracellular antibacterial targets and associated inhibitors directly in living cells.

Journal of the American Chemical Society
Merck & Co., Inc., Rahway, NJ, USA (United States) (US), University of Southampton (GB)
Partnerships for the goals
Openalex Percentile: Top 14%
Chemical Synthesis and Analysis
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Identification of Antibacterial Cyclic Peptides with a High-Throughput Cell-Based Dropout Screen — Leonie M. Windeln, Ali Tavassoli, et al. · Journal of the American Chemical Society (2026) | TGRS Research Map | TGRS