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Updated: May 21, 2026

Antimicrobial Peptides Produced by Selective Pressure Incorporation of Non-canonical Amino Acids
Published on: May 4, 2018
A novel cyclic antimicrobial peptide N1-7567 targets Campylobacter jejuni through membrane disruption and metabolic
Xuesong Zhang1, Jikai Ren2, Qian Gao2
1College of Life Sciences, Hainan Normal University, Haikou, 571158, China; Jiangsu Key Lab of Zoonosis/Jiangsu Co-innovation Center for Prevention and Control of Important Animal Infectious Diseases and Zoonoses, Yangzhou University, 48 Wenhui East Road, Yangzhou, Jiangsu, 225000, China; Key Laboratory of Prevention and Control of Biological Hazard Factors (Animal Origin) for Agri-food Safety and Quality, Ministry of Agriculture of China, Yangzhou University, 48 Wenhui East Road, Yangzhou, Jiangsu, 225000, China.
Abstract:
Campylobacter jejuni (C. jejuni) is a prominent foodborne pathogen commonly associated with poultry, representing a potential concern for global public health. Here, we identified a novel cyclic antimicrobial peptide, N1-7567, encoded by a noncanonical small open reading frame (ORF) in a Bacillus licheniformis (B. licheniformis) isolate. N1-7567 (AFLKRFSCRLIRAGKYLSCLLQPAA) adopts a cyclic conformation formed by a disulfide bond between two cysteine residues. N1-7567 exhibited a minimum inhibitory concentration (MIC) against C. jejuni of 64 μg/mL. Studies revealed that N1-7567 associates with the bacterial membrane, disrupts bacterial membrane integrity, and subsequently penetrates into the cytoplasm. This process triggers nitric oxide (NO) release, reactive oxygen species (ROS) accumulation, adenosine triphosphate (ATP) leakage, and direct interaction with bacterial genomic DNA, collectively leading to bacterial growth inhibition. Notably, N1-7567 significantly reduced Galleria mellonella mortality. Together, these findings highlight N1-7567 as a promising candidate for controlling C. jejuni infection and transmission.
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