• Bulletin of the Korean Chemical Society
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• 제20권9호
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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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• 제32권11호
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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.

• 한국동물학회:학술대회논문집
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• 한국동물학회 1996년도 공동 춘계학술대회
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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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• 제31권1호
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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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• 제30권1호
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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.

• 한국환경과학회지
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• 제6권2호
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• pp.189-194
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• 1997

Hornet venom의 독성 peptide인 mastoparan과 mastoparan-B를 solid phase peptide syn- thesis method로 합성한 후 이들과 phospholipid와의 상호작용, 이들의 항균 활성 및 용혈 활성 을 조사하였다. 두가지 독성 peptide 모두 중성 liposome에서 저 농도에서도 dye release를 유도할 수 있었다. 중성 liposome에 대한 mastoparan-B의 결합 친화도는 산성 liposome에서 보다 작았다. Mastoparan과 mastoparan-B는 두가지 모두 그람 양성 세균에 대하여 강한 항균 활성을 가지고 있었으나 그람 음성 세균에 대해서는 각각 약하거나 유력한 활성을 보였다. Mastoparan과 mastoparan-B는 5$\mu$M의 낮은 농도에서도 적혈구를 분해시키는 독성을 보였다.

• 한국생물물리학회:학술대회논문집
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• 한국생물물리학회 1999년도 학술발표회 진행표 및 논문초록
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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)

• 한국생물공학회:학술대회논문집
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• 한국생물공학회 2000년도 추계학술발표대회 및 bio-venture fair
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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.

• 한국수산과학회지
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• 제55권6호
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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%).