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 serovar Typhimurium TISTR 292 and serovar Enteritidis DMST 15679 with a MIC value of 2 mM. In contrast, . serovar Newp...

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Bibliographic Details
Published in:Antibiotics (Basel) 2024-01, Vol.13 (1), p.19
Main Authors: Pimchan, Thippawan, Tian, Fu, Thumanu, Kanjana, Rodtong, Sureelak, Yongsawatdigul, Jirawat
Format: Article
Language:English
Subjects:
Amino acids
Animals
Antibacterial agents
Antibiotics
Antiinfectives and antibacterials
Antimicrobial agents
antimicrobial peptide
Antimicrobial peptides
Aqueous solutions
Bacteria
Cell membranes
Confocal microscopy
Contamination
Drug resistance
egg yolk protein
Electron microscopy
Ethical aspects
Fatty acids
food-borne pathogens
Fourier transforms
Hydrolysates
Infections
Infrared spectroscopy
Iodides
Leakage
Lipids
Membrane permeability
Membranes
Microscopy
Minimum inhibitory concentration
Mode of action
Nucleic acids
Oxytetracycline
Peptides
Permeability
Propidium iodide
Proteins
Salmonella
Salmonella Typhimurium
Spectrum analysis
Synchrotrons
Toxicity
Yolk
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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 serovar Typhimurium TISTR 292 and serovar Enteritidis DMST 15679 with a MIC value of 2 mM. In contrast, . serovar Newport ATCC 6962 and other strains of Typhimurium and Enteritidis were inhibited at 4 mM. EYHp6 increased the cell membrane permeability of . 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 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 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 . .
ISSN:2079-6382
2079-6382
DOI:10.3390/antibiotics13010019