• Applied Chemistry for Engineering
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• v.20 no.3
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• pp.251-257
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• 2009

Recently, there is much interest in the antimicrobial activity of silver since silver has known to be safe and effective as a disinfectant or an antimicrobial agent against a broad spectrum of microorganisms. Although silver has been applied to various kinds of products due to the effective antimicrobial activity, the quantitative antimicrobial activity or detailed mechanism of silver is not clearly investigated yet, causing the controversy and confusion. In this review paper, we summarized the characteristics, antimicrobial activities and mechanisms, synergistic effects with other antimicrobials, and applicability of silver.

• Microbiology and Biotechnology Letters
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• v.39 no.1
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• pp.1-8
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• 2011

The antimicrobial effects of silver (Ag) ion or salts are well known. Recently, silver nanoparticle is attracting an interest in a wide variety of fields since it has been known to be safe and effective as an antimicrobial agent against a broad spectrum of microorganisms. Although silver nanoparticle has been applied to various kinds of products owing to its potent antimicrobial activity, the effects of silver nanoparticle on microorganisms and antimicrobial mechanism have not been revealed clearly. In this paper, we summarized the characteristics, antimicrobial activities and mechanisms, cytotoxicity and applicability of silver nanoparticle.

• Journal of Microbiology and Biotechnology
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• v.25 no.6
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• pp.759-764
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• 2015

Antimicrobial peptides (AMPs) are one of the critical components in host innate immune responses to imbalanced and invading microbial pathogens. Although the antimicrobial activity and mechanism of action have been thoroughly investigated for decades, the exact biological properties of AMPs are still elusive. Most AMPs generally exert the antimicrobial effect by targeting the microbial membrane, such as barrel stave, toroidal, and carpet mechanisms. Thus, the mode of action in model membranes and the discrimination of AMPs to discrepant lipid compositions between mammalian cells and microbial pathogens (cell selectivity) have been studied intensively. However, the latest reports suggest that not only AMPs recently isolated but also well-known membrane-disruptive AMPs play a role in intracellular killing, such as apoptosis induction. In this mini-review, we will review some representative AMPs and their antimicrobial mechanisms and provide new insights into the dual mechanism of AMPs.

• Microbiology and Biotechnology Letters
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• v.38 no.1
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• pp.19-23
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• 2010

Recently, marine organisms are emerging as a leading group for identifying and extracting novel bioactive substances. These substances are known to possess a potential regarding not only as a source of pharmaceutical products but also their beneficial effects on humans. Among the substances, antimicrobial peptides (AMPs) specifically have attracted considerable interest for possible use in the development of new antibiotics. AMPs are characterized by relatively short cationic peptides containing the ability to adopt a structure in which cationic or hydrophobic amino acids are spatially scattered. Although a few reports address novel marine organisms-derived AMPs, their antimicrobial mechanism(s) are still remain unknown. In this review, we summarized the peptides previously investigated, such as Pleurocidin, Urechistachykinins, Piscidins and Arenicin-1. These peptides exhibited significant antimicrobial activities against human microbial pathogens without remarkable hemolytic effects against human erythrocytes, and their mode of actions are based on permeabilization of the plasma membrane of the pathogen. Therefore, the study of antimicrobial peptides derived from marine organisms may prove to be useful in the design of future therapeutic antimicrobial drugs.

• Journal of Microbiology and Biotechnology
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• v.29 no.11
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• pp.1707-1716
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• 2019

The development of new antimicrobial agents is essential for the effective treatment of diseases such as sepsis. We previously developed a new short peptide, Pap12-6, using the 12 N-terminal residues of papiliocin, which showed potent and effective antimicrobial activity against multidrug-resistant Gram-negative bacteria. Here, we investigated the antimicrobial mechanism of Pap12-6 and a newly designed peptide, Pap12-7, in which the 12^th Trp residue of Pap12-6 was replaced with Val to develop a potent peptide with high bacterial selectivity and a different antibacterial mechanism. Both peptides showed high antimicrobial activity against Gram-negative bacteria, including multidrug-resistant Gram-negative bacteria. In addition, the two peptides showed similar anti-inflammatory activity against lipopolysaccharide-stimulated RAW 264.7 cells, but Pap12-7 showed very low toxicities against sheep red blood cells and mammalian cells compared to that showed by Pap12-6. A calcein dye leakage assay, membrane depolarization, and confocal microscopy observations revealed that the two peptides with one single amino acid change have different mechanisms of antibacterial action: Pap12-6 directly targets the bacterial cell membrane, whereas Pap12-7 appears to penetrate the bacterial cell membrane and exert its activities in the cell. The therapeutic efficacy of Pap12-7 was further examined in a mouse model of sepsis, which increased the survival rate of septic mice. For the first time, we showed that both peptides showed anti-septic activity by reducing the infiltration of neutrophils and the production of inflammatory factors. Overall, these results indicate Pap12-7 as a novel non-toxic peptide with potent antibacterial and anti-septic activities via penetrating the cell membrane.

• The Journal of the Korean dental association
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• v.41 no.2 s.405
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• pp.116-123
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• 2003

Antimicrobial Peptides are natural antibiotics evolved by many plants, invertebrate, and vertebrate to defend against the microbial infection. Antimicrobial peptides show a broad-spectrum antimicrobial activity with little opportunity for the development of resistance since they target microbial membranes that distinguish microbes from enkaryotic cells. The oral cavity is constantly exposed to microbial challenges and antimicrobial peptides play an important role in managing the oral health. With the increase of resistant micro-organisms to conventional antibiotics, antimicrobial peptides are attracting interests as novel antibiotics. In this review, the characteristics of antimicrobial of antimicrobial peptides including the classification, mechanism of action, resistance, and expression in the oral cavity have been discussed in the prospects of application to oral disease.

• Journal of the Korean Society of Food Science and Nutrition
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• v.29 no.6
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• pp.1112-1115
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• 2000

• Microbiology and Biotechnology Letters
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• v.51 no.3
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• pp.243-249
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• 2023

We recently found that the insect-derived antimicrobial peptide CopA3 (LLCIALRKK) directly binds to and inhibits the proteolytic activation of caspases, which play essential roles in apoptotic processes. However, the mechanism of CopA3 binding to caspases remained unknown. Here, using recombinant GST-caspase-3 and -6 proteins, we investigated the mechanism by which CopA3 binds to caspases. We showed that replacement of cysteine in CopA3 with alanine caused a marked loss in its binding activity towards caspase-3 and -6. Exposure to DTT, a reducing agent, also diminished their interaction, suggesting that this cysteine plays an essential role in caspase binding. Experiments using deletion mutants of CopA3 showed that the last N-terminal leucine residue of CopA3 peptide is required for binding of CopA3 to caspases, and that C-terminal lysine and arginine residues also contribute to their interaction. These conclusions are supported by binding experiments employing direct addition of CopA3 deletion mutants to human colonocyte (HT29) extracts containing endogenous caspase-3 and -6 proteins. In summary, binding of CopA3 to caspases is dependent on a cysteine in the intermediate region of the CopA3 peptide and a leucine in the N-terminal region, but that both an arginine and two adjacent lysines in the C-terminal region of CopA3 also contribute. Collectively, these results provide insight into the interaction mechanism and the high selectivity of CopA3 for caspases.

• Applied Chemistry for Engineering
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• v.21 no.4
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• pp.366-371
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• 2010

Accompanying the rapid advance of nanotechnology, various nano-particles have shown promise as strong antimicrobial agents against a broad spectrum of microorganisms. These nanoparticles also have potential applications in medical devices, water treatments systems, environmental sensors and so on. However, with increasing concerns about the impact of engineered nanoparticles, many researchers are recently reporting the cytotoxicity of nanoparticles. In this review paper, we summarized the antimicrobial activities and mechanisms of various kinds of engineered nanoparticles to imprale understanding about these characteristics of nanoparticles.

• KSBB Journal
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• v.27 no.1
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• pp.9-15
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• 2012

Antimicrobial peptides are widely used in various organisms as a defense system against infection. The peptides are lethal towards bacteria and fungi, however have minimal toxicity in mammalian and plant cells. In this aspect, it is considered that antimicrobial peptides are new alternative materials for defensing against microbial infection. Here, we describe overall characteristics of antimicrobial peptides based on the mechanism of action, classification of the peptides, report detection/screening methods and chemical/biological production. It is expected that understanding of innate immune system based on antimicrobial peptides tends to develop novel natural antimicrobial agents, which might be applied for defensing pathogenic microorganisms resistant to conventional antibiotics.