• Bulletin of the Korean Chemical Society
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• v.20 no.9
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• pp.1073-1077
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• 1999

CRAMP, a 37-amino acid cationic antimicrobial peptide was recently deduced from the cDNA cloned from mouse femoral marrow RNA. In order to investigate the structure-activity relationship and functional region of CRAMP, CRAMP and its 18-mer overlapping peptides were synthesized by the solid phase method. CRAMP showed broad spectrum antibacterial activity against both Gram-positive and Gram-negative bacterial strains (MIC: 3.125-6.25 μM) but had no hemolytic activity until 50 μM. CRAMP was found to have a potent anticancer activity (IC50: 12-23 μM) against two human small cell lung cancer cell lines. Furthermore, CRAMP was found to display faster bactericidal rate in B. subtilis rather than E. coli in the kinetics of bacterial killing. Among 18-meric overlapping fragment peptides, only CRAMP (16-33) displayed potent antibacterial activity (MIC: 12.5-50 μM) against several bacteria with no hemolytic activity. Circular dichroism (CD) spectra anal-ysis indicated that CRAMP and its analogues will form the amphipathic α-helical conformation in the cell membranes similar to other antimicrobial peptides, such as cecropins and magainins.

• Journal of Microbiology and Biotechnology
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• v.32 no.11
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• pp.1382-1389
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• 2022

Asterias pectinifera, a species of starfish and cause of concern in the aquaculture industry, was recently identified as a source of non-toxic and highly water-soluble collagen peptides. In this study, we investigated the antioxidant and anti-photoaging functions of compounds formulated using collagen peptides from extracts of Asterias pectinifera and Halocynthia roretzi (AH). Our results showed that AH compounds have various skin protective functions, including antioxidant effects, determined by measuring the scavenging activity of 2,2-diphenyl-1-picrylhydrazyl radicals, as well as anti-melanogenic effects, determined by measuring tyrosinase inhibition activity. To determine whether ethosome-encapsulated AH compounds (E(AH)) exert ultraviolet (UV)-protective effects, human dermal fibroblasts or keratinocytes were incubated with E(AH) before and after exposure to UVA or UVB. E(AH) treatment led to inhibition of photoaging-induced secretion of matrix metalloproteinase-1 and interleukin-6 and -8, which are associated with inflammatory responses during UV irradiation. Finally, the antibacterial effects of AH and E(AH) were confirmed against both gram-negative and gram-positive bacteria. Our results indicate that E(AH) has the potential for use in the development of cosmetics with a range of skin protective functions.

• Proceedings of the Zoological Society Korea Conference
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• 1996.04a
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• pp.58.2-58
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• 1996

No Abstract, See Full Text

• The Plant Pathology Journal
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• v.31 no.1
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• pp.1-11
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• 2015

Antimicrobial cyclic peptides derived from microbes bind stably with target sites, have a tolerance to hydrolysis by proteases, and a favorable degradability under field conditions, which make them an attractive proposition for use as agricultural fungicides. Antimicrobial cyclic peptides are classified according to the types of bonds within the ring structure; homodetic, heterodetic, and complex cyclic peptides, which in turn reflect diverse physicochemical features. Most antimicrobial cyclic peptides affect the integrity of the cell envelope. This is achieved through direct interaction with the cell membrane or disturbance of the cell wall and membrane component biosynthesis such as chitin, glucan, and sphingolipid. These are specific and selective targets providing reliable activity and safety for non-target organisms. Synthetic cyclic peptides produced through combinatorial chemistry offer an alternative approach to develop antimicrobials for agricultural uses. Those synthesized so far have been studied for antibacterial activity, however, the recent advancements in powerful technologies now promise to provide novel antimicrobial cyclic peptides that are yet to be discovered from natural resources.

• Journal of Dairy Science and Biotechnology
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• v.30 no.1
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• pp.37-44
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• 2012

Milk-derived bioactive peptides have been found to exhibit various physiological activities such as angiotensin-converting enzyme (ACE) inhibitory, antibacterial, and antioxidative effects. Bioactive peptides can be used in the formulation of functional foods, nutraceuticals, and natural drugs because of their beneficial effects. However, the degree of variability in the composition, functionality, and sensory properties of such peptides has greatly limited their use in the food industry. In this review, we discuss the main peptides obtained from milk proteins and summarize findings from previous studies on the production and biological activities of these peptides. In addition, we compare the methods used to separate and identify the structure of the bioactive peptides and highlight current investigations into engineering and implementation of technologies that would allow more efficient isolation of bioactive peptides for functional food production. To improve human health, further molecular biology studies will also be required to elucidate the complex network of interactions between food microorganisms and the digestive system.

• Journal of Environmental Science International
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• v.6 no.2
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• pp.189-194
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• 1997

Toxic peptides from hornet venom, mastoparan and mastoparan-B were synthesized us- ing the solid phase peptide synthesis method and investigated the interaction of them with phospholipid bilayer, antibacterial activity, and hemolytic activity. Both toxic peptides could induce dye release at a low concentration in neutral liposome. The binding affinity of mastoparan-B for neutral liposome was smaller than that for acidic one. Mastoparan and mastoparan-B had strong antibacterial activity for gram-positive bacteria, but weak or potent activity for gram-negative ones, respectively. Mastoparan and mastoparan-B lysed erythrocyte very little up to 5 $\mu$M.

• Proceedings of the Korean Biophysical Society Conference
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• 1999.06a
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• pp.32-32
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• 1999

Cecropin A(1-8)-magainin 2(1-12) and cecropm A(1-8)-melittin(1-12) hybrid peptides were known to have potent antitumor and antibacterial activity. In particular, cecropm A(l-8)-magainin 2(1-12) has powerful antibacterial and antitumor activity with no hemolytic effect.(omitted)

• Korean Journal of Agricultural Science
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• v.51 no.3
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• pp.341-350
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• 2024

According to various negative effects of antibiotic growth promoters, the effects of nature-derived alternatives to antibiotic growth promoters are mainly investigated in livestock industry these days. The effects of nature-derived alternatives to antibiotic growth promoters are mainly investigated in livestock industry these days. This study was conducted to estimate the efficiency of natural-derived alternatives to antimicrobial and antioxidant such as oregano oil (OGO), sulfide type antimicrobial peptides derived from Bacillus or Yeast (SAPBY), antimicrobial peptides derived from yeast (APY). The lactic acid bacteria growth effects were found to be minimal. The antibacterial activity of SAPBY was minimal, but OGO and APY showed antibacterial activity against Escherichia coli and Salmonella Typhimurium, and APY also showed antibacterial activity against Staphylococcus. Antioxidant effects were observed in all SAPBY, OGO, and APY, and when comparing the radical scavenging rate at 10 mg·mL^-1 for each sample, OGO showed the highest at 84.9%, followed by SAPBY at 48.7%. Therefore, the substances that can be used as natural antibiotics are SAPBY, APY, and OGO. It is believed that adding these substances to feed and feeding them to livestock will greatly contribute to improving the health of livestock and the productivity of safe livestock products. In further, research focused on various nature-derived alternatives to antibiotic growth promoter in livestock industry is needed.

• 한국생물공학회:학술대회논문집
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• 2000.11a
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• pp.669-671
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• 2000

Antimicrobial cationic peptides have attracted increasing research and clinical interest as a natural antibiotics due to their broad spectrum of antimicrobial activites and the rapid development of multidrug-resistant pathogenic microorganisms. In this study, first, we synthesized artificial fusion partner and cationic peptide genes (lactoferricin, magainin, protegrin-1, and indolicidin). Second, we constructed recombinant expression vectors and then transformed Pichia pastoris. Finally, expressed cationic peptides were purified and tested for their antimicrobial activites. Antimicrobial activity has been tested upon the appearance of clearing zone on the plate with the lawn of gram negative E.coli XL- I blue and garm positive Staphylococcus aureus. Protegrin-1 and Indolicidin have apparant activity of cationic peotides. This fusion technique may lead to a general and suitable tool for production of pure antimicrobial cationic peptides in Pichia pastoris.