• Bulletin of the Korean Chemical Society
• /
• v.35 no.9
• /
• pp.2809-2812
• /
• 2014

The 43-residue defensin-like peptide coprisin, which is isolated from dung bettle, Copris tripartitus, is a potent antimicrobial peptide. In our previous work, we determined the tertiary structure of coprisin and found that alpha helical region of coprisin from residue 19 to residue 30 is important for its antimicrobial activities. Here, we designed cop12mer and cop9mer analogs of coprisin based on the tertiary structure of coprisin. To investigate the relationship between hydrophobicity and antimicrobial activities and develop the potent peptide antibiotics, we designed cop9mer-1 with substitution of $His^2$ with Trp in cop9mer. The results showed that cop9mer-1 has higher toxicities as well as improved antimicrobial activities compared to cop9mer. In order to reduce the toxicity of cop9mer-1, we designed cop9mer-2 and cop9mer-3 with substitution of $Cys^3$ with Lys or Ser. Substitution of $Cys^3$ with these hydrophilic amino acids results in lower cytotoxicities compared to cop9mer-1. Cop9mer-2 with substitution of $Cys^3$ with Lys in Cop9mer-1 showed high antibacterial activities against drug resistant bacteria without cytotoxicity. Antibiotic action of cop9mer-1 analog appears to involve permeabilization of the bacterial cell membrane while cop9mer-2 and cop9mer-3 may have different mechanism of action. These results imply that that optimum balance in hydrophobicity and hydrophilicity in these 9-meric peptides plays key roles in their antimicrobial activities as well as cytotoxicities.

• Food Science and Preservation
• /
• v.14 no.2
• /
• pp.183-187
• /
• 2007

The antimicrobial properties of methanolic extract (PML) from Prunus nune byproducts after liquor manufacturing weremeasured using various putrefactive and food spoilage microorganisms. PML showed remarkable antimicrobial effects against various putrefactive and food spoliage microorganisms when used at 500g/mL. The antimicrobial properties were stable for 30 min at 100C and at pH 3 11. PML seems to be a natural antimicrobial agent with high effectiveness, and shows both thernal and pH stability. In addition, the mode of antimicrobial action suggests that the active components may synergistically perturb microbial membrane functions.

• Proceedings of the Korean Society of Dyers and Finishers Conference
• /
• 2009.03a
• /
• pp.112-113
• /
• 2009

• Journal of Food Hygiene and Safety
• /
• v.7 no.2
• /
• pp.99-106
• /
• 1992

To prevent food-poisoning outbreaks by Vibrio vulnificus the antimicrobial efficacy of grapefruit seed extract (GFSE) was examined. Minimal inhibitory concentration (in vitro) for the microorganism was found to be 50∼100 ppm. Transmission electron micrographs of Vibrio vulnificus showed the biocidal action of this natural antimicrobial agent would be related to specific respiratory effect coupled with the destruction of permeable function of microbial cell membrane. After Anguilla japonica GFSE-injected to the body was incubated in the seawater contaminated by Vibrio vulnifiucs the fish meats were taken up, mixed with control diet and used as a diet in the feeding experiment. In this experiment the effect of GFSE treated with fish muscle on body weight, protein efficiency ratio, serum enzymes and serum blood components of broiler chicks was investigated. It is proved from this study that there is neither Vibriosis nor toxicity associated with GFSE itself an fish meats treated with it when it is injected to the fish body at a level of 250 ppm or less.

• Food Science and Preservation
• /
• v.12 no.1
• /
• pp.8-16
• /
• 2005

To develop natural antimicrobial agents for extending the self-life of Kimchi, the effect of botanical antimicrobial agent-citrus products(BAAC) on microorganisms related to Kimchi spoilage was investigated. The inhibitory effect of BAAC on microorganisms related to Kimchi spoilage was increased according to the concentration of BAAC. Antimicrobial activities of BAAC against microoiganisms related to Kimchi spoilage were remarkably high. The effect of BAAC on the cellular membrane function of microorganisms showed the perturbation of cells in the presence of BAAC. Direct isualization of microbial cells by using both transmission md scanning electron microscope showed microbial cell membrane was destroyed by treating with BAAC. It could be confirmed that BAAC completely inhibit the growth of the test strains. The pH of BAAC-added Kimchi was a little higher than that of the control through the fermentation period. Titratable acidify, vitamin C and viable cells in BAAC-added Kimchi were changed more slowly than those in the control. Sensory evaluation did not show any significant difference between $0.01\%$ BAAC-added Kimchi and the control that showed the best palatabilities during fermentation.

• Bulletin of the Korean Chemical Society
• /
• v.32 no.5
• /
• pp.1645-1649
• /
• 2011

[ ${\beta}$ ]Ketoacyl acyl carrier protein synthase I (KAS I) is involved in the elongation of unsaturated fatty acids in bacterial fatty acid synthesis and a therapeutic target of designing novel antibiotics. In this study, we performed receptor-oriented pharmacophore-based in silico screening of E. coli KAS I (ecKAS I) with the aim of identifying novel inhibitors. We determined one pharmacophore map and selected 8 compounds as candidates ecKAS I inhibitors. We discovered one antimicrobial compound, YKAe1008, N-(3-pyridinyl) hexanamide, displaying minimal inhibitory concentration (MIC) values in the range of 128-256 ${\mu}g/mL$ against MRSA and VREF. YKAe1008 was subsequently assessed for binding to ecKAS I using saturation-transfer difference NMR spectroscopy. Further optimization of this compound will be carried out to improve its antimicrobial activity and membrane permeability against bacterial cell membrane.

• Journal of the Korean Magnetic Resonance Society
• /
• v.15 no.1
• /
• pp.1-13
• /
• 2011

9Pbw2 is a 9-mer analog of protaetiamycine derived from the larvae of the beetle Protaetia brevitarsis. Previously, we designed four 9-mer peptide analogues to optimize the balance between the hydrophobicity and cationicity of the peptides and to increase bacterial cell selectivity. Among them, 9Pbw2 has high antibacterial activity without cytotoxicity. The results obtained in previous study suggest that the bactericidal action of 9Pbw2 may be attributed to the inhibition of the functions of intracellular components after penetration of the bacterial cell membrane. In order to understand structure-activity relationships, we determined the three-dimensional structure of 9Pbw2 in 200 mM DPC micelle by NMR spectroscopy. 9Pbw2 has one hydrophobic turn helix from $Trp^3$ to $Arg^8$ and positively charged residues at the N- and C-terminus. This result suggested that positively charged residues from position at the C-terminus in 9Pbw2 may be important for the primary binding to the negatively charged phospholipid head groups in bacterial cell membranes and hydrophobic residues in the middle portion face toward the acyl chains of the hydrophobic lipid in the bacterial cell membrane.

• Journal of Microbiology and Biotechnology
• /
• v.20 no.8
• /
• pp.1185-1188
• /
• 2010

Previously, papiliocin was isolated from the swallowtail butterfly Papilio xuthus and its antimicrobial activity was suggested. In this study, the antifungal mechanism of papiliocin against Candida albicans was investigated. Confocal laser scanning microscopy (CLSM) and 1,6-diphenyl-1,3,5-hexatriene (DPH) fluorescence analysis indicated that papiliocin disturbed the fungal plasma membrane. Moreover, the assessment of the release of FITC-dextran (FD) from liposomes further demonstrated that the antifungal mechanism of papiliocin could have originated from the pore-forming action and that the radius of the pores was presumed to be anywhere from 2.3 to 3.3 nm.

• Animal Bioscience
• /
• v.34 no.9
• /
• pp.1525-1531
• /
• 2021

Objective: The objective of this study was to evaluate the antimicrobial effects of fermented Maillard reaction products made by milk proteins (FMRPs) on Clostridium perfringens (C. perfringens), and to elucidate antimicrobial modes of FMRPs on the bacteria, using physiological and morphological analyses. Methods: Antimicrobial effects of FMRPs (whey protein plus galactose fermented by Lactobacillus rhamnosus [L. rhamnosus] 4B15 [Gal-4B15] or Lactobacillus gasseri 4M13 [Gal-4M13], and whey protein plus glucose fermented by L. rhamnosus 4B15 [Glc-4B15] or L. gasseri 4M13 [Glc-4M13]) on C. perfringens were tested by examining growth responses of the pathogen. Iron chelation activity analysis, propidium iodide uptake assay, and morphological analysis with field emission scanning electron microscope (FE-SEM) were conducted to elucidate the modes of antimicrobial activities of FMRPs. Results: When C. perfringens were exposed to the FMRPs, C. perfringens cell counts were decreased (p<0.05) by the all tested FMRPs; iron chelation activities by FMRPs, except for Glc-4M13. Propidium iodide uptake assay indicate that bacterial cellular damage increased in all FMRPs-treated C. perfringens, and it was observed by FE-SEM. Conclusion: These results indicate that the FMRPs can destroy C. perfringens by iron chelation and cell membrane damage. Thus, it could be used in dairy products, and controlling intestinal C. perfringens.

• Korean Journal of Fisheries and Aquatic Sciences
• /
• v.55 no.6
• /
• pp.875-885
• /
• 2022

This study was performed to confirm the optimal extraction method for antimicrobial peptides from the Hard-shelled mussel. Extractions were performed with two processes including 1% HAc/boiling and 1% HAc/non-boiling methods and used extracts for the comparison of the antimicrobial activity, protease stability, action mechanism, AU-PAGE (acid-urea PAGE), and HPLC chromatograms. 1% HAc/boiling extract showed potent antibacterial activities both against Gram-positive and negative bacterium but 1% HAc/non-boiling extract showed antibacterial activity only against Gram-positive bacteria. Treatment of 1% HAc/boiling extract with proteases retained almost antibacterial activity against B. subtilis, but abolished significant antibacterial activity against E. coli D31. Only 1% HAc/boiling extract showed two discrete clearing antibacterial zones including slow migrating and rapid migrating zones. Both extracts showed strong DNA-binding ability but did not show bacterial membrane permeabilizing ability. In comparison of the chromatogram obtained from C₁₈ or cation-exchange HPLC, the eluted peaks from 1% HAc/boiling extract showed high hydrophobic property or absorbance compared to 1% HAc/non-boiling extract, respectively. The concentration of the purified antimicrobial peptide was also higher in 1% HAc/boiling extract than in 1% HAc/non-boiling extract. Our results suggest that the effective extraction condition for antimicrobial peptides from marine invertebrate is boiling process in a weak acetic acid solution (1%).