• Korean Journal of Environmental Biology
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• v.36 no.4
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• pp.601-609
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• 2018

Microcystis aeruginosa, a freshwater cyanobacteria species known to be one of the most predominant species responsible for cyanobacterial harmful algal blooms (CyanoHABs). It has been frequently associated with the contamination of neurotoxins and peptide hepatotoxins, such as microcystin and lipopolysaccharides-LPSs. CyanoHABs control technologies so far put in place do not provide a fundamental solution and cause secondary pollution linked with the control measures. For this study, algicidal peptides, which have been reported to be non-toxic and to have antimicrobial properties, were employed for the development of novel eco-friendly control against CyanoHABs. The four peptides (CMA1, CMA2, HPA3P, and HPA3NT3) selected in this study showed significant algicidal effects against M. aeruginosa cells inducing cell aggregation and flotation. Moreover, the newly generated peptides (K160242-5) with certain modifications also displayed high algicidal activity. The algicidal activity of the peptides was found to depend on the concentrations and structures of each of amino acid. The results of this study suggested a novel possibility of CyanoHABs control using the non-toxic algicidal peptides.

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

• Bulletin of the Korean Chemical Society
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• v.17 no.3
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• pp.239-244
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• 1996

Mastoparan B (MP-B) that is a novel MP isolated from the hornet Vespa basalis, was studied as compared with MP, in terms of interaction with phospholipid bilayer and antimicrobial activity. MP-B has more hydrophilic amino acid residues in hydrophilic face of amphiphilic α-helical structure than MP. The both peptides exhibited considerably different effect on interaction with lipid bilayers, e.g. their conformation in the presence of acidic and neutral liposomes, dye-release ability from encapsulated liposomes, but on the whole the interaction mode was similar. On antimicrobial activity, MP had a strong activity against Gram-positive bacteria but no against Gram negative ones. Contrary to this, MP-B had a strong activity against Gram-positive and potent against Gram-negative ones. Since both peptides have almost same residues on the hydrophobic side, such more hydrophilic surface on the molecule seems to lead to the subtle change in its interaction with membranes, resulting in the alternation in its biological activity.

• Food Science of Animal Resources
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• v.35 no.6
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• pp.831-840
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• 2015

Functionally and physiologically active peptides are produced from several food proteins during gastrointestinal digestion and fermentation of food materials with lactic acid bacteria. Once bioactive peptides (BPs) are liberated, they exhibit a wide variety of physiological functions in the human body such as gastrointestinal, cardiovascular, immune, endocrine, and nervous systems. These functionalities of the peptides in human health and physiology include antihypertensive, antimicrobial, antioxidative, antithrombotic, opioid, anti-appetizing, immunomodulatory and mineral-binding activities.

• Journal of Dairy Science and Biotechnology
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• v.28 no.1
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• pp.43-52
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• 2010

In addition to the nutritional values, milk has a wide range of bioactive compounds which have been found to be increasingly important for physiological and biochemical functions on human metabolism and health. Bioactive components in milk comprise specific proteins, peptides, lipids and carbohydrates. Especially, milk proteins are known to exert a wide range of nutritional, functional, and biological activities. And milk proteins are considered the most important source of bioactive peptides, including antihypertensive, antithrombotic, antimicrobial, antioxidative, immunomodulatory, and opioid peptides. Many ingredients containing specific bioactive peptides derived from milk protein hydrolysates have been launched on the market and are currently under development. In future studies more emphasis should be given to the health-promoting effect in the well-defined human clinical studies for the successful development of function foods based on the milk-derived bioactive components.

• Microbiology and Biotechnology Letters
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• v.24 no.5
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• pp.529-533
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• 1996

Melittin (ME) from honeybee venom has a broad range of strong antimicrobial activity, but it has hemolytic activity against eukaryotic cells. In order to design peptides with powerful antifungal activity without cytotoxic property of ME and understand structure-antifungal activity relationships, the hybrid peptides derived from the sequences of ME and cecropin A (CA) or magainin 2 (MA), MA(10-17)ME(1-12) and CA(1-8)ME(1-12). were synthesized by solid phase method. MA(10-17)ME(1-12) showed potent antifungal activity comparable to ME against Fusarium oxysporum with no hemolytic activity against human red blood cells. The hybrid peptides showed strong inhibi- tion of (1, 3)-$\beta$-D-glucan synthase. This result indicates that the antifungal activity of the hybrid peptides against Fusarium oxysporum is attributed to the inhibition of cell wall synthesis. The results therefore showed a successful design of a peptide having antifungal activity without hemolytic property.

• Journal of Microbiology and Biotechnology
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• v.27 no.4
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• pp.759-767
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• 2017

Lactophoricin (LPcin), which is a part of proteose peptone isolated from bovine milk, is a cationic amphipathic ${\alpha}-helical$ antimicrobial peptide. Its truncated variants and mutated analogs were designed and their antimicrobial activities were evaluated by using various assays, like broth dilution methods and disk diffusion methods as well as hemolysis assay. Three analogs, LPcin-C8 (LPcin-YK1), LPcin-T2&6W (LPcin-YK2), and LPcin-T2&6W-C8 (LPcin-YK3), which showed better antibiotic activities than LPcin, were selected. Their secondary structures were also characterized by using CD spectropolarimetry. These three analogs of LPcin could be used as an alternative source of powerful antibacterial agents.

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 2004.06a
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• pp.161-162
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• 2004

• Proceedings of the Zoological Society Korea Conference
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• 1998.10b
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• pp.254.1-254
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• 1998

No Abstract, See Full Text

• Proceedings of the Korean Magnetic Resonance Society Conference
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• 2001.02a
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• pp.25-25
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• 2001