• Proceedings of the Zoological Society Korea Conference
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• 2000.04a
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• pp.79.2-79
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• 2000

No Abstract, See Full Text

• Proceedings of the Zoological Society Korea Conference
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• 2000.04a
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• pp.78.2-78
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• 2000

No Abstract, See Full Text

• Bulletin of the Korean Chemical Society
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• v.35 no.9
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• pp.2818-2824
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• 2014

Trp residue is considered as one of the important constituents in antimicrobial peptides (AMPs) as it presence secured good activities in many cases. However, it is preferable to be changed because of their sensitivity towards light. We have synthesized the short Trp-rich AMP Pac-525 and its analogues to investigate the possibility of His(chx) as possible replacement analogue for Trp in AMPs. Based on the assay result of the antibacterial activity including anti-MRSA activity, His(chx) is considered as good candidate for the Trp replacement. Through these study, we found that His(chx) had several merits to design therapeutic antimicrobial agents compare to Trp in terms of i) increasing antibacterial activity without hemolytic activity, ii) successful in designing the short peptide (only four residues), iii) having anti-MRSA activity, iv) overcoming the light sensitivity. Furthermore, transmission electron microscopy (TEM) and dye leakage experiments suggested that P11 and P16 containing His(chx) kill bacteria via forming pore/ion channels on bacterial cell membranes.

• Korean Journal of Microbiology
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• v.36 no.3
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• pp.236-241
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• 2000

A defensin is an inducible antibacterial peptide from a fleshfly and contains 40 residues basic peptide with six cysteines. For the consiruction of recombinant S cerevisiae expressing defensin, the structural gene coding for active defensin was chemically synthesized and fused in fiam to GAP promoter, MFul preprosequence and the GAL7 transcription terminator, generating a recombinant plasnlid pGMD18. S. ce~evisine 2805 Gells were transror~ned to uracil prototroph by the pGMDl8 arid the transformed cells showing antibacterial activity against 111. luteus TAM1056 were selected by growth inhibition zone assay. The optimal culture conditions for the unprovement of the defensin production of a selected tmdonnant were investigated. The optirmzed medium containing 0.4% yeast extract, 2% corn steep liquor, 2.5% glucose and 0.05% $C_2CO_3$, could be determined and the optimum lemperature. and initial pH could be detennnied as $28^{\circ}C$ and pH 3, ~mpectively. The optimized conditioiis revealed the trvofold Increase in the cell growth and the fourfold in the antibaclerial activity. coinpar-ed with tllc Yl'D medium.

• Bulletin of the Korean Chemical Society
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• v.27 no.7
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• pp.1075-1078
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• 2006

• Proceedings of the Korean Biophysical Society Conference
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• 2001.06a
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• pp.29-29
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• 2001

Leukocytes are important elements in the host defense against microbial infections. A variety of antimicrobial peptides named as the cathelicidin family have been identified from leukocytes. PMAP-23 derived from porcine myeloid cells is an antimicrobial peptide belong to the cathelicidin family. PMAP-23 was reported to have potent growth inhibition activity against bacterial and tumor cells with no hemolytic activity.(omitted)

• Journal of Veterinary Science
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• v.24 no.3
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• pp.44.1-44.17
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• 2023

Background: Antibiotic resistance is a significant public health concern around the globe. Antimicrobial peptides exhibit broad-spectrum and efficient antibacterial activity with an added advantage of low drug resistance. The higher water content and 3D network structure of the hydrogels are beneficial for maintaining antimicrobial peptide activity and help to prevent degradation. The antimicrobial peptide released from hydrogels also hasten the local wound healing by promoting epithelial tissue regeneration and granulation tissue formation. Objective: This study aimed at developing sodium alginate based hydrogel loaded with a novel antimicrobial peptide Chol-37(F34-R) and to investigate the characteristics in vitro and in vivo as an alternative antibacterial wound dressing to treat infectious wounds. Methods: Hydrogels were developed and optimized by varying the concentrations of crosslinkers and subjected to various characterization tests like cross-sectional morphology, swelling index, percent water contents, water retention ratio, drug release and antibacterial activity in vitro, and Pseudomonas aeruginosa infected wound mice model in vivo. Results: The results indicated that the hydrogel C proved superior in terms of cross-sectional morphology having uniformly sized interconnected pores, a good swelling index, with the capacity to retain a higher quantity of water. Furthermore, the optimized hydrogel has been found to exert a significant antimicrobial activity against bacteria and was also found to prevent bacterial infiltration into the wound site due to forming an impermeable barrier between the wound bed and external environment. The optimized hydrogel was found to significantly hasten skin regeneration in animal models when compared to other treatments in addition to strong inhibitory effect on the release of pro-inflammatory cytokines (interleukin-1β and tumor necrosis factor-α). Conclusions: Our results suggest that sodium alginate -based hydrogels loaded with Chol-37(F34-R) hold the potential to be used as an alternative to conventional antibiotics in treating infectious skin wounds.

• BMB Reports
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• v.42 no.9
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• pp.586-592
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• 2009

The bactenecin is an antibacterial peptide with an intramolecular disulfide bond. We recently found that homodimeric bactenecin exhibits more potent antibacterial activity than the monomeric form and retains its activity at physiological conditions. Here we assess the difference in the modes of antibiotic action of homodimeric and monomeric bactenecins. Both monomeric and dimeric bactenecins almost completely killed both Staphylococcus aureus and E. coli within 10-30 min at concentrations of $8-16\;{\mu}M$. However, exposure to liposomes elicited an increase in the fluorescence quantum yield from a tryptophan-containing monomeric analog, while the homodimeric analog showed a significant reduction in fluorescence intensity. Moreover, unlike the monomer, the homodimer displayed apparent membrane-lytic activity enabling release of various sized dyes from liposomes, and rapidly and fully depolarized the S. aureus membrane. Together, our results suggest that homodimeric bactenecin forms pores in the bacterial membrane, while monomeric one penetrates through the membrane to target intracellular molecules/organelles.

• International Journal of Industrial Entomology and Biomaterials
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• v.31 no.2
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• pp.85-89
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• 2015

This peptide has antibacterial activity against several Gram-positive and Gram-negative bacteria. Bombyx mori cecropinB1(BmCecB1) is antimicrobial peptides from Bombyx mori and belongs to cecropin family. Antimicrobial peptides are important components of the innate immune systems in all living organism. To produce the BmCecB1 antimicrobial peptide, we constructed transgenic silkworm that expressed BmCecB1 gene under the control BmA3 promoter using piggyBac vector. The use of the 3xP3-driven EGFP cDNA as a marker allowed us to rapidly distinguish transgenic silkworm. Mixtures of the donor vector and helper vector were micro-injected into 600 eggs of bivoltin silkworms, Baegokjam. In total, 49 larvae (G0) were hatched and allowed to develop into moths. The resulting G1 generation consisted of 22 broods, and we selected 2 broods containing at least 1 EGFP-positive embryo. The rate of successful transgenesis for the G1 broods was 9%. We identified 9 EGFP-positive G1 moths and these were backcrossed with wild-type moths. With the aim of identifying a BmCecB1 as antimicrobial peptide, we investigated the Radical diffusion Assay (RDA) and then demonstrated that BmCecB1 possesses high antibacterial activities against Gram-negative bacteria.

• Journal of Microbiology and Biotechnology
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• v.25 no.10
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• pp.1629-1633
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• 2015

Peptide assimilation in Helicobacter pylori necessitates a coordinated working of the peptide transport systems (PepTs) and aminopeptidase (PepA). We found that H. pylori hydrolyzes two detector peptides, _L-phenylalanyl- _L-3-thiaphenylalanine (PSP) and _L-phenylalanyl- _L-2-sulfanilylglycine (PSG), primarily before intake and excludes their antibacterial effects, whereas Escherichia coli readily transports them with resultant growth inhibition. PSP assimilation by H. pylori was inhibited by aminopeptidase inhibitor bestatin, but not by dialanine or cyanide-m-chlorophenylhydrazone, contrary to that of E. coli. RT- and qRT-PCR analyses showed that H. pylori may express first the PepTs (e.g., DppA and DppB) and then PepA. In addition, western blot analysis of PepA suggested that the bacterium secretes PepA in response to specific inducers.