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. 2025 Jul 1:16:1622282.
doi: 10.3389/fmicb.2025.1622282. eCollection 2025.

In vitro and in vivo anti- Pseudomonas aeruginosa activity of a scorpion peptide derivative

Zhongjie Li  1 , Jiao Zhang  1 , Yabo Liu  1 , Qi Dai  1 , Shasha Li  1 , Bo Deng  1 , Pengfei Wu  1 , Wanwu Li  1 , Yanfang Dong  1 , Pengyang Xin  2 , Wenlu Zhang  1
Affiliations

In vitro and in vivo anti- Pseudomonas aeruginosa activity of a scorpion peptide derivative

Zhongjie Li et al. Front Microbiol. .

Abstract

Introduction: Pseudomonas aeruginosa is an important opportunistic and foodborne disease-related bacterium, and the increasing antibiotic resistance of the pathogen leads to the urgent exploration of new and effective antibacterial agents. In this study, a scorpion peptide derivative HTP2 was designed.

Methods: The in vitro anti-P. aeruginosa activity was evaluated using a broth microdilution assay. A mouse model of P. aeruginosa skin subcutaneous infection was used to evaluate the in vivo anti-P. aeruginosa activity of HTP2. The antibacterial mechanism and influence on pathogenic factors of P. aeruginosa of HTP2 were also investigated.

Results: HTP2 could effectively inhibit the growth of P. aeruginosa cells with low hemolytic activity. HTP2 killed P. aeruginosa in a concentration-dependent manner, and could damage the membrane, induce ROS accumulation, and interact with nucleic acids. HTP2 could also inhibit biofilm formation, motility, pyocyanin production, and elastase activity of P. aeruginosa. In the mouse subcutaneous infection model, HTP2 significantly reduced the bacterial load of P. aeruginosa cells and inhibited inflammatory infiltration in the infection area.

Conclusion: HTP2 could effectively kill P. aeruginosa in vitro and in vivo, and had the potential as an anti-P. aeruginosa agent.

Keywords: Pseudomonas aeruginosa; antimicrobial peptide; food contamination; scorpion; skin infection.

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Conflict of interest statement

The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

Figures

Figure 1
Figure 1
Peptides and in vitro activities. (A) Characterization and helical wheel diagram. (B) Anti-P. aeruginosa activity. (C) Hemolytic activity. (D) Stability and competition binding assay. GRAVY (Grand average of hydropathicity): Determined by ProtParam (https://web.expasy.org/protparam/). μH (Hydrophobic moment) and helical wheel diagram: Determined by the Heliquest (https://heliquest.ipmc.cnrs.fr/cgi-bin/ComputParams.py).
Figure 2
Figure 2
Anti-P. aeruginosa mechanism of HTP2. (A) Time-killing kinetics. Negative control group, 0.9% saline. (B) Confocal fluorescence microscopic images of P. aeruginosa cells treated with FITC-HTP2. (C) Membrane integrity measurement. Negative control group, 0.9% saline. RFU: Relative fluorescence unit. (D) Membrane potential measurement. Negative control group, 0.9% saline. RFU: Relative fluorescence unit. (E) ROS measurement. Negative control group, 0.9% saline. RFU: Relative fluorescence unit. *p < 0.05. (F) Nucleic acids binding assay. (a) P. aeruginosa RNA; (b) pET-28a; Ratio of peptide/nucleic acids: line 1 (0:1), line 2 (5:1), line 3 (10:1), line 4 (20:1).
Figure 3
Figure 3
Influence of HTP2 on pathogenic factors of P. aeruginosa. (A) Biofilm formation. *p < 0.05. (B) Swimming motility assay. (C) Pyocyanin production. *p < 0.05. (D) Elastase activity. *p < 0.05.
Figure 4
Figure 4
In vivo anti-P. aeruginosa activity of HTP2. (A) Hematoxylin–Eosin staining for the negative control group. (B) Hematoxylin–Eosin staining for the HTP2 treatment group. (C) Hematoxylin–Eosin staining for the Ciprofloxacin treatment group. (D) CFU per gram of the tissue. Negative control group, 0.9% saline. *p < 0.05.
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