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Peer-reviewedCC BYAntibiotics (Basel, Switzerland)

Cell-Penetration Peptide-Conjugated Octominin II Hybrid Inhibits the Multidrug-Resistant Shigella flexneri.

  • Jayasinghage Nirmani Chathurnagika Jayasinghe1
  • Chamilani Nikapitiya1
  • Vijaya R Dirisala2
  • Tae-Won Kim1
  • Mahanama De Zoysa1
  • Ilson Whang3
  1. 1College of Veterinary Medicine, Chungnam National University, Daejeon 34134, Republic of Korea.
  2. 2Department of Biotechnology, School of Biotechnology and Pharmaceutical Sciences, Vignan's Foundation for Science, Technology and Research, Guntur 522213, Andhra Pradesh, India.
  3. 3National Marine Biodiversity Institute of Korea (MABIK), 75, Seochun-gun 33662, Chungchungnam-do, Republic of Korea.
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Abstract

Background/Objectives: The genus Shigella is one of the major pathological agents responsible for diarrhea and diarrhea-related mortality worldwide. It shows a decreasing sensitivity to most conventional antibiotics available today. Methods: Hence, an antimicrobial peptide, Octominin II, was conjugated to a cell-penetrating peptide (HIV-TAT) named TAT-Octominin II, and its antibacterial effect against Shigella flexneri was investigated. Results: TAT-Octominin II displayed minimum inhibitory and bactericidal concentrations of 10 and 25 µg/mL, respectively. It showed rapid membrane-permeabilizing activity, as observed in the ONPG assay. TAT-Octominin II treatment altered the cell membrane integrity and causing membrane damage in S. flexneri. Moreover, TAT-Octominin II increased oxidative stress, as evidenced by the upregulation of antioxidant genes, such as sodA, sodB, katG, oxyR, and soxR. Furthermore, TAT-Octominin II bound to genomic DNA and RNA, which likely inhibited the transcription and translation of bacterial proteins. In addition, TAT-Octominin II possessed lipopolysaccharide neutralization activity. In vitro toxicity analysis was performed using mammalian Raw 264.7 and HEK 293 cells, which showed no toxicity at lower concentrations (0-100 µg/mL). Conclusions: Overall, our results demonstrate that TAT-conjugated Octominin II exhibits enhanced antibacterial activity compared to Octominin II alone, suggesting that TAT-mediated delivery of AMPs could be a promising strategy to improve the therapeutic efficacy of AMPs.

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Cite

BibTeXRIS
BibTeX
@article{jayasinghe2026cellpenetration,
  title = {{Cell-Penetration Peptide-Conjugated Octominin II Hybrid Inhibits the Multidrug-Resistant Shigella flexneri.}},
  author = {Jayasinghage Nirmani Chathurnagika Jayasinghe and Chamilani Nikapitiya and Vijaya R Dirisala and Tae-Won Kim and Mahanama De Zoysa and Ilson Whang},
  journal = {Antibiotics (Basel, Switzerland)},
  year = {2026},
  month = oct,
  doi = {10.3390/antibiotics15101033},
  url = {https://europepmc.org/article/MED/42938774},
  note = {CC BY},
}
RIS
TY  - JOUR
TI  - Cell-Penetration Peptide-Conjugated Octominin II Hybrid Inhibits the Multidrug-Resistant Shigella flexneri.
AU  - Jayasinghage Nirmani Chathurnagika Jayasinghe
AU  - Chamilani Nikapitiya
AU  - Vijaya R Dirisala
AU  - Tae-Won Kim
AU  - Mahanama De Zoysa
AU  - Ilson Whang
PY  - 2026
DA  - 2026/10/16
JO  - Antibiotics (Basel, Switzerland)
DO  - 10.3390/antibiotics15101033
UR  - https://europepmc.org/article/MED/42938774
AB  - Background/Objectives: The genus Shigella is one of the major pathological agents responsible for diarrhea and diarrhea-related mortality worldwide. It shows a decreasing sensitivity to most conventional antibiotics available today. Methods: Hence, an antimicrobial peptide, Octominin II, was conjugated to a cell-penetrating peptide (HIV-TAT) named TAT-Octominin II, and its antibacterial effect against Shigella flexneri was investigated. Results: TAT-Octominin II displayed minimum inhibitory and bactericidal concentrations of 10 and 25 µg/mL, respectively. It showed rapid membrane-permeabilizing activity, as observed in the ONPG assay. TAT-Octominin II treatment altered the cell membrane integrity and causing membrane damage in S. flexneri. Moreover, TAT-Octominin II increased oxidative stress, as evidenced by the upregulation of antioxidant genes, such as sodA, sodB, katG, oxyR, and soxR. Furthermore, TAT-Octominin II bound to genomic DNA and RNA, which likely inhibited the transcription and translation of bacterial proteins. In addition, TAT-Octominin II possessed lipopolysaccharide neutralization activity. In vitro toxicity analysis was performed using mammalian Raw 264.7 and HEK 293 cells, which showed no toxicity at lower concentrations (0-100 µg/mL). Conclusions: Overall, our results demonstrate that TAT-conjugated Octominin II exhibits enhanced antibacterial activity compared to Octominin II alone, suggesting that TAT-mediated delivery of AMPs could be a promising strategy to improve the therapeutic efficacy of AMPs.
SN  - 2079-6382
ER  -