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Journal of Semnan University of Medical Sciences

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Cover image of the article: Assessment of the Antibacterial Activity of the Recombinant Protein Ib- AMP4 on Acinetobacter baumannii (ATCC19606) Under in vitro Conditions

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Outline

https://doi.org/10.69107/koomesh-153624

Assessment of the Antibacterial Activity of the Recombinant Protein Ib- AMP4 on Acinetobacter baumannii (ATCC19606) Under in vitro Conditions

Authors

Majid SafariMajid Safari ORCID1, Hamid AbtahiHamid Abtahi ORCID2,*, Shima ChehreiiShima Chehreii ORCID1, Shohreh FahimiradShohreh Fahimirad ORCID2
1Department of Microbiology, Arak Branch, Islamic Azad University, Arak, Iran
2Molecular and Medicine Research Center, Arak University of Medical Sciences, Arak, Iran
*Corresponding Author: Molecular and Medical Research Center, Arak University of Medical Sciences, Arak, Iran. Tel: +98- 8634173502, Fax: +98-8634173526, Email:abtahi@arakmu.ac.ir
Koomesh:Vol. 27, issue 5; e153624
Published online:Sep 21, 2025
Article type:Research Article
How to Cite:Safari M, Abtahi H, Chehreii S, Fahimirad S. Assessment of the Antibacterial Activity of the Recombinant Protein Ib- AMP4 on Acinetobacter baumannii (ATCC19606) Under in vitro Conditions. Koomesh. 2025;27(5):e153624. doi: https://doi.org/10.69107/koomesh-153624

Abstract

Background: Acinetobacter baumannii is a common pathogen found in hospital settings, recognized for its significant resistance to various antibiotics. In the fight against multidrug-drug resistant (MDR) pathogens, researchers are investigating the potential of antimicrobial peptides sourced from natural antibiotics.

 

 

Objectives: This study aimed to evaluate the antibacterial efficacy of the recombinant protein impatiens balsamina-antimicrobial peptide (IbAMP4) against A. baumannii (ATCC 19606) in a controlled laboratory environment.

 

 

Methods: The recombinant protein Ib-AMP4 was synthesized by inserting the gene responsible for encoding Ib-AMP4 into the Escherichia coli BL21(DE3) strain through transformation using the pET32a vector. The purification of the protein was optimized using Nickel-Nitrilotriacetic acid (Ni-NTA) affinity chromatography. The efficacy of Ib-AMP4 was assessed by determining its minimum inhibitory concentration (MIC), analyzing bacterial growth kinetics, and evaluating its antibacterial activity against A. baumannii (ATCC19606).

 

 

Results: The recombinant Ib-AMP4 produced in E. coli BL21 exhibited notable antimicrobial efficacy against A. baumannii, with a MIC established at 111 μg/mL. When applied at a concentration twice that of the MIC, Ib-AMP4 markedly decreased both viable cell counts and turbidity, as demonstrated by bacterial growth kinetics and antibacterial assays, achieving a purity level greater than 70%.

 

 

Conclusion: The research illustrated the antibacterial efficacy of the recombinant protein Ib-AMP4 against A. baumannii. These results offer encouraging opportunities for the development and production of novel antimicrobial agents aimed at addressing infections induced by A. baumannii.

 

 

Highlights

KeywordsAntibacterial PeptidesRecombinant ProteinsIb-AMP4 PeptideAcinetobacter baumanniiAntimicrobial Peptides

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Copyright

© 2025, Author(s). This open-access article is available under the Creative Commons Attribution 4.0 (CC BY 4.0) International License (https://creativecommons.org/licenses/by/4.0/), which allows for unrestricted use, distribution, and reproduction in any medium, provided that the original work is properly cited.

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