# Peptides from Drosophila sleep protein Nemuri halt bacterial protein synthesis in cell-level tests, including drug-resistant strains

- Published: 2026-11-11 09:54 UTC
- Section: Life & Health › Biotechnology
- Tags: Nemuri peptides, antimicrobial peptides, drug-resistant bacteria, ribosomal condensation, bacterial protein synthesis, biomolecular condensates, Escherichia coli, Staphylococcus aureus, University of Tsukuba, Nature Communications
- URL: https://realtech.media/news/rt-aae4904098cf7dcd330281cd_peptides_from_drosophila/

**Researchers at the University of Tsukuba and Hokkaido University derived Nemuri peptides that condense ribosome-rich regions in bacteria. The work is at the laboratory stage; animal infection models are still needed.**

![Peptides from Drosophila sleep protein Nemuri halt bacterial protein synthesis in cell-level tests, including drug-resistant strains](https://realtech.media/media/2026/11/879e2f930352d304.jpg)
*Joydeep, Wikimedia Commons, CC BY-SA 3.0*

A team from the University of Tsukuba and Hokkaido University reported short antimicrobial peptides derived from Nemuri, a sleep-inducing protein of *Drosophila melanogaster*. The work was published in Nature Communications on 29 October 2026. According to the authors, the peptides inhibit the growth of a wide range of microorganisms, including drug-resistant pathogens [1].

## Mechanism: ribosomal condensation

In *Escherichia coli* and *Staphylococcus aureus*, the peptides, called Nemuri peptides, also showed bactericidal activity at concentrations close to those needed to inhibit growth [1]. They are intrinsically disordered. They enter bacterial cells and accumulate in ribosome- and RNA-rich regions, and no substantial membrane disruption was detected at antimicrobial concentrations under the conditions tested [1].

Inside the cell, the peptides bind broadly to RNA and to ribosomal surfaces through multivalent interactions. This remodels ribosome-rich regions into condensates with reduced ribosomal mobility and suppresses global protein synthesis [1]. The authors note that this distinguishes the peptides from canonical antibiotics that target a specific site on the ribosome [1].

## Toxicity and open questions

The peptides showed low cytotoxicity toward Drosophila and mammalian cells in culture [1]. The authors conclude that the organization and material dynamics of bacterial ribosomes can serve as a biophysical vulnerability exploitable by antimicrobial peptides [1].

The results come from laboratory experiments on bacterial and cultured cells. The release from the University of Tsukuba states that evaluation of efficacy and safety in animal models of bacterial infection is still required. Until such studies are done, the Nemuri peptides can be regarded only as a starting point for developing agents against drug-resistant bacteria, as the developers describe them.

The corresponding authors are Hirofumi Toda of the International Institute for Integrative Sleep Medicine at the University of Tsukuba and N. Nobuo Noda of the Institute for Genetic Medicine at Hokkaido University. The study addresses antibiotic resistance, which the paper describes as a global health threat requiring antimicrobials with alternative modes of action [1].

## Sources

1. [Nature Communications](https://doi.org/10.1038/s41467-026-78960-5)
2. [EurekAlert](https://www.eurekalert.org/news-releases/1151207)

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Source: RealTech, realtech.media — https://realtech.media/news/rt-aae4904098cf7dcd330281cd_peptides_from_drosophila/