Volume 9, Issue 4 (2023)                   IEM 2023, 9(4): 0-0 | Back to browse issues page

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Ghaznavi-Rad E, Sadoogh Abbasian2 A, Sadoogh Abbasian S, Zarei-Mehrvarz E, Abtahi H. The LL37-rIb-AMP4 antimicrobial peptide as a treatment for systematic infection of Pseudomonas aeruginosa, Acinetobacter baumannii, Methicillin-resistant Staphylococcus aureus (MRSA) and Vancomycin-resistant Enterococci (VRE) cells in a mouse model.. IEM 2023; 9 (4)
URL: http://iem.modares.ac.ir/article-4-71409-en.html
1- Molecular and Medical Research Center, Arak University of Medical Sciences, Arak, Iran.
2- Department of Internal Medicine, School of Medicine, Amiralmomenin Hospital, Arak University of Medical Sciences, Arak, Iran.
3- Molecular and Medical Research Center, Arak University of Medical Sciences, Arak, Iran. , habtahi2001@yahoo.com
Abstract:   (242 Views)

Aims: Antimicrobial peptides (AMPs) are beneficial compounds that could be used as a new and effective method to suppress microbes. Both Ib-AMP4 and LL37 are antimicrobial peptides with a wide range of antimicrobial activities. This research aimed to evaluate the antibacterial potential of LL37-rIb-AMP4 hybrid protein as an antimicrobial agent against pathogenic bacteria. Therefore, its antibacterial effects against Acinetobacter baumannii, Pseudomonas aeruginosa, vancomycin-resistant Enterococcus (VRE), and methicillin-resistant Staphylococcus aureus (MRSA) were investigated in vivo and in vitro.

Materials & Methods: In this study, antimicrobial peptides rIb-AMP4, LL37, and LL37-rIb-AMP4 were expressed, purified, and refolded, and their synergistic and antibacterial effects in combination with each other (LL37+rIb-AMP4) and as fusion proteins (LL37-rIb-AMP4) were tested against A. baumannii, P. aeruginosa, VRE, and MRSA cells in vitro (MIC, time kill, and SEM) and against P. aeruginosa and VRE cells in vivo.
Findings: LL37-rIb-AMP4 Protein with molecular weight= 28 KD was correctly produced and purified. Despite the lack of synergistic effects between LL37 and rIb-AMP4 peptides in vitro, the stability test results showed higher stability for LL37-rIb-AMP4 hybrid protein.
The findings of in vivo tests confirmed that all infected mice were improved with LL37-rIb-AMP4 and no signs of bacteria were observed in their blood and spleen samples. Also, these results confirmed the stability and higher activity of LL37-rIb-AMP4 than the single form of these proteins.
Conclusion: Considering the antimicrobial potential of the produced proteins, it seems that the recombinant LL37-rIb-AMP4 protein could be considered and used as a stable and active antimicrobial drug in future studies.
     
Article Type: Original Research | Subject: Bacteriology
Received: 2023/09/5 | Accepted: 2024/01/30 | Published: 2024/02/5

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