Anti-Salmonella Activity of a Novel Peptide, KGGDLGLFEPTL, Derived from Egg Yolk Hydrolysate
The present study aimed to characterize the mode of action of a novel antimicrobial peptide isolated from egg yolk hydrolysate. The EYHp6, KGGDLGLFEPTL, exhibited inhibition against <i>Salmonella enterica</i> serovar Typhimurium TISTR 292 and <i>S. enterica</i> serovar Enteri...
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| Main Authors: | , , , , |
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| Format: | Book |
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MDPI AG,
2023-12-01T00:00:00Z.
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| Online Access: | Connect to this object online. |
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| Summary: | The present study aimed to characterize the mode of action of a novel antimicrobial peptide isolated from egg yolk hydrolysate. The EYHp6, KGGDLGLFEPTL, exhibited inhibition against <i>Salmonella enterica</i> serovar Typhimurium TISTR 292 and <i>S. enterica</i> serovar Enteritidis DMST 15679 with a MIC value of 2 mM. In contrast, <i>S</i>. <i>enterica</i> serovar Newport ATCC 6962 and other strains of Typhimurium and Enteritidis were inhibited at 4 mM. EYHp6 increased the cell membrane permeability of <i>S</i>. Typhimurium TISTR 292, leading to DNA leakage. Membrane integrity determined by propidium iodide and SYTO9 staining visualized by confocal microscopy demonstrated that EYHp6 at 1 × MIC induced disruption of cell membranes. Electron microscopy revealed that treatment of <i>S.</i> Typhimurium with EYHp6 led to damage to the cell membrane, causing the leakage of intracellular contents. Synchrotron-based Fourier-transform infrared spectroscopy indicated that EYHp6 killed <i>S.</i> Typhimurium by targeting fatty acids and nucleic acids in the cell membrane. The peptide did not show hemolytic activity up to 4 mM. These findings suggest that EYHp6 could be a promising antibacterial agent for controlling the growth of <i>S</i>. <i>enterica</i>. |
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| Item Description: | 10.3390/antibiotics13010019 2079-6382 |