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Int J Mol Sci
2018 Oct 05;1910:. doi: 10.3390/ijms19103041.
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Antibacterial and Antibiofilm Activity and Mode of Action of Magainin 2 against Drug-Resistant Acinetobacter baumannii.
Kim MK
,
Kang N
,
Ko SJ
,
Park J
,
Park E
,
Shin DW
,
Kim SH
,
Lee SA
,
Lee JI
,
Lee SH
,
Ha EG
,
Jeon SH
,
Park Y
.
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Antimicrobial peptides (AMPs) are promising therapeutic agents for treating antibiotic-resistant bacterial infections. Previous studies showed that magainin 2 (isolated from African clawed fogs Xenopus laevis) has antimicrobial activity against gram-positive and gram-negative bacteria. The present study was conducted to investigate the antibacterial activity of magainin 2 against Acinetobacter baumannii. Magainin 2 showed excellent antibacterial activity against A. baumannii strains and high stability at physiological salt concentrations. This peptide was not cytotoxic towards HaCaT cells and showed no hemolytic activity. Biofilm inhibition and elimination were significantly induced in all A. baumannii strains exposed to magainin 2. We confirmed the mechanism of magainin 2 on the bacterial outer and inner membranes. Collectively, these results suggest that magainin 2 is an effective antimicrobial and antibiofilm agent against A. baumannii strains.
Figure 1. Structure analysis of magainin 2. (A) Helical wheel diagram of the peptide. The projection was obtained from http://heliquest.ipmc.cnrs.fr/cgibn/ComputParam.py. Positively charged residues are represented in blue, while hydrophobic residues are shown as yellow circles. The N-terminal and C-terminal parts are represented in red letters “N†and “Câ€. (B) Three-dimensional structure of magainin 2.
Figure 2. Circular dichroism (CD) spectra of magainin 2. (A) The peptide was measured in TFE, which mimics the hydrophobic environment of the microbial membrane and (B) SDS, which mimics the negatively charged prokaryotic membrane environment.
Figure 3. Cytotoxicity and hemolytic activity of magainin 2. (A) Hemolytic activity of peptides against mouse red blood cells (RBCs). (B) Cytotoxicity of peptides against HaCaT cells.
Figure 4. Effect of Acinetobacter baumannii biofilm formation by magainin 2. (A) Quantitative measurements of biofilm formation using crystal violet staining. (B) Inhibitory effect of peptides on biofilm formation. Antibiotics (ciprofloxacin and gentamicin) and buforin 2 were used as controls.
Figure 5. EVOS2 images of Acinetobacter baumannii biofilm stained with SYTO9 dye (green fluorescence).
Figure 6. Biofilm reduction assay. (A) Degree of biofilm removal by magainin 2, ciprofloxacin, and gentamicin using crystal violet staining. (B) Image of removed biofilm after treatment with 256 µM of peptide and antibiotics. (C) SYTO9-stained biofilm image.
Figure 7. Magainin 2 mechanism of action. (A,B) The outer membrane permeability of magainin 2 was measured using NPN dye. (C,D) Depolarization of cytoplasmic membrane induced by magainin 2, determined using the membrane potential-sensitive fluorescent dye DisC3-5. (A,C: Acinetobacter baumannii KCTC 2508, B,D: Acinetobacter baumannii 907233).
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