• Title/Summary/Keyword: K-13 펩타이드

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A Study on the Use of Human Antibacterial Peptide LL-37-derived FK-13 as a Cosmetic Preservative (인간 항균펩타이드인 LL-37 유래의 FK-13의 화장품보존제로 활용에 대한 연구)

  • Yun, Hyo-Suk;Choe, Yong-Joon;Yang, Jae-Chan;Min, Hye-Jung
    • Journal of the Korean Applied Science and Technology
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    • v.38 no.6
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    • pp.1568-1576
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    • 2021
  • Here, we conducted the study on the possibility of using FK-13, a short analog of human-derived antibacterial peptide LL-37, as a cosmetic preservative to discover a natural cosmetic preservative that is safe for human body. For the purpose, FK-13 composed of 13 amino acids was synthesized by solid-phase peptide synthesis, and purified using reversed phase-high performance liquid chromatography (RP-HPLC). The purity and molecular weight were confirmed by liquid chromatography-mass spectrometry (LC-MS) analysis. FK-13 showed high antimicrobial activity on the three gram-positive bacteria (Staphylococcus aureus, Bacillus subtilis, and Staphylococcus epidermidis), the three gram-negative bacteria (Escherichia coli, Salmonella typhimurium, and Pseudomonas aeruginosa), and also even the fungus Candida glabrata. FK-13 had a broad spectrum of antibacterial activity, showing a suitability as a cosmetic preservative. In addition, FK-13 showed high thermostability and higher antibacterial activity in a comparative test with existing natural herbal cosmetic and chemical preservatives. Therefore, as FK-13 is a safe material and has high antibacterial activity at a low concentration, it is likely to be applied as a peptide natural cosmetic preservative that can replace existing chemical preservatives.

A Novel Screening Strategy for Salt-resistant Alpha-helical Antimicrobial Peptides from a Phage Display Library (Phage Display Library를 이용한 Salt-Resistant Alpha-Helical 항균 펩타이드의 새로운 탐색방법)

  • Park, Ju-Hee;Han, Ok-Kyung;Lee, Baek-Rak;Kim, Jeong-Hyun
    • Microbiology and Biotechnology Letters
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    • v.35 no.4
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    • pp.278-284
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    • 2007
  • A novel screening strategy for salt-resistant antimicrobial peptides from a M13 peptide library was developed. Fusion of MSI-344, a magainin derivative and indolicidin to pIII coat proteins did not significantly affect viability of the recombinant phages, which indicated that the pIII could neutralize toxicity of the antimicrobial peptides and therefore it is possible to construct antimicrobial peptide library in Escherichia coli. On the basis of the conserved sequence of ${\alpha}$-helical antimicrobial peptides, a semi-combinatorial peptide library was constructed in which the peptides were displayed by pIII. To remove hemolytic activity from the library, the phages bound to red blood cells were removed, and the subtracted phage library was screened for binding to target bacteria Pseudomonas aeruginosa and Staphylococcus aureus under high salt concentrations. The screened peptides showed relatively low antimicrobial activity against the target bacteria. However, antimicrobial activities of the screened peptides P06 and S18 were not affected by the cation concentrations of 150 mM $Na^+$, 2 mM $Mg^{2+}$ and 2 mM $Ca^{2+}$ without significant hemolytic activity. This screening strategy that is based on binding capacity to target cells provides new potential to develop salt-tolerant antimicrobial peptides.

Design of Short Indolicidin Analogs with Enhanced Prokaryotic Selectivity (증가된 원핵세포선택성을 가진 짧은 인돌리시딘 유사체의 설계)

  • Shin, Song Yub
    • Microbiology and Biotechnology Letters
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    • v.40 no.4
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    • pp.409-413
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    • 2012
  • Indolicidin (ID) is a 13-residue Trp-rich antimicrobial peptide (AMP) isolated from bovine neutrophils. In addition to having a high antimicrobial potency, it is also toxic to mammalian cells. To develop novel ID-derived AMPs with shorter lengths and enhanced prokaryotic selectivities (meaning potent antimicrobial activity against bacterial cells without toxicity against mammalian cells) over the parental ID, several ID analogs were designed and synthesized. Finally, 10-residue ID analogs (SI, SI-PA, SI-WF and SI-WL) with much higher prokaryotic selectivity than the parental ID were developed. Our results suggest that the hydrophobic and aromatic amino acids at the central position of the analog SI with the highest prokaryotic selectivity are important for potent antimicrobial activity, but two Pro residues do not affect antimicrobial activity. The order of prokaryotic selectivity for ID and its designed analogs was SI > SI-PA > SI-WF > SI-WL > ID > SI-WA. Taken together, our designed short ID analogs could be developed as therapeutic agents for treating bacterial infections.

Antifreeze Activity of Dimerized Type I Antifreeze Protein Fragments (Type I 결빙방지 단백질 조각 이량체의 결빙방지 활성)

  • Kim, Hak Jun
    • Journal of Life Science
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    • v.27 no.5
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    • pp.584-590
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    • 2017
  • Antifreeze proteins (AFPs) bind to ice crystals and inhibit their growth. AFPs are essential for the survival of organisms living in subzero environments. Type I AFP (AFP37) isolated from winter flounder is an ${\alpha}$-helical peptide of 37 residues long. In this study, we attempted to develop short AFP fragments with higher activity and solubility. We designed and synthesized N-terminal 15 and 21 residue-long AFPs, designated AFP15 and 21. Also dimerized AFP15 and 21, designated dAFP15N and dAFP21N, respectively, were generated through disulfide bonds between peptides containing CGG residues added to the N-terminus of AFP15 and AFP21 (designated AFP15N and 21N). Their helical contents and antifreeze activities were assessed using circular dichroism (CD) spectroscopy and a nanoliter osmometer, respectively. The helical content of AFP15 AFP21, AFP15N, AFP21N, dAFP15N and dAFP21N was 47, 48, 23.8, 28, 49.1, and 52%, respectively compared to that of wild type AFP37; the antifreeze activity was 8.4, 9.3, 0.05, 5.6, 12.1, 11.2% respectively, compared to that of wild type AFP37. Contrary to our anticipation, the dimerized peptides showed almost the same antifreeze activity as their monomeric counterparts. These results indicate that the dimerized peptides behave as monomeric peptides due to the high rotational freedom of disulfide bonds connecting two monomeric peptides. The star-shaped ice crystals generated by the peptides also demonstrated weak interaction between ice and peptides.

Gly-His-Lys Conjugated Chitosan and its Cell Proliferation Effects (Gly-His-Lys 펩타이드가 결합된 키토산과 그의 세포증식 효과에 관한 연구)

  • Ha Byung-Jo;Lee Yoon-Sik;Park Soo Nam
    • Journal of the Society of Cosmetic Scientists of Korea
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    • v.30 no.3 s.47
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    • pp.399-404
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    • 2004
  • Novel GHK-conjugated chitosan was prepared by the solid-phase method using $N^{\alpha}-Fmoc$ amino acids/BOP coupling reagent. For this purpose, the chitosan microbeads which had a mean diameter of 70 um were prepared by the W/O emulsion-phase separation method. The GHK was successfully coupled to the chitosan microbeads by stepwise solid-phase method. The result of amino aid analysis was in good agreement with the theoretical values; $Gly_{1.02}\;of\;His_{1.13}\;Lys_{0.96).$. The cell proliferation effect of the GHK-bound chitosan microbeads was measured by MTT assay. We concluded that GHK-bound chitosan microbeads gave higher cell Proliferation effect than chitosan microbeads.

Optimization of Peptides Production Derived from By-product Viscera of Yoensan Ogae Meat Process (연산 오계 부산물 내장육으로부터 펩타이드 생산 최적 공정 개발과 생산물의 특성 분석)

  • Ji, Joong Gu;Yoo, Sun Kyun
    • Journal of the Korean Applied Science and Technology
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    • v.33 no.3
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    • pp.549-559
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    • 2016
  • Korean Black body fowl (Gallus gallus domesticus; Ogae) designated as a natural monument (registration number 265) has been known as a superb traditional Korean medicine. In this study, The production of peptide from the Viscera Waste of Yeonsan Ogae was optimized using commercial protease (bromelain) by response surface methodology under high pressure process. The range of processes was pressure (30 to 100 MPa), reaction time (1 to 5 h), and substrate concentration (10 to 30%, w/v). After reaction, the degree of hydrolysis, distribution of amino acids, and molecular weight of peptides were investigated. As a results, the optimization conditions were pressure 90 MPa, reaction time 3 to 4 h, and the amount of viscera meat 20% (w/v), respectively. The molecular weight of protein hydrolysates was distributed 400 to 1,000 Da. Accordingly we presumed that most products were peptides. Of those peptides, nonpolar or hydrophobic, polar but uncharged, positively charged, and negatively charged amino acids were 42.03, 26.0, 13.3, and 18.6%, respectively. Because higher amount of hydrophobic amino acids, we expected that those products would be able to utilize as the functional food ingredients.

Studies on the Properties of Enzymatic Hydrolysates from File-fish (말쥐치 단백의 효소 가수분해물의 특성에 관한 연구)

  • Suh, Hyung-Joo;Chung, Soo-Hyun;Son, Jong-Youn;Lee, Hyo-Ku;Bae, Song-Whan
    • Korean Journal of Food Science and Technology
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    • v.28 no.4
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    • pp.678-683
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    • 1996
  • The purpose of this study was to elucidate characteristics of hydrolysates from file-fish flesh with various proteases. File-fish flesh was chopped, homogenized with water, and hydrolysed by 8 different kinds of commercially available protease. High production of peptide was observed in bromelain and neutrase treatment. On the other hand, large amount of free amino acid was observed in esp/sav and pronase treatment. Neutrase and pancreatin hydrolysate contained large amount of 5'-GMP. Organoleptic studies showed that the bromelain, esp/sav and protease hydrolysate had strong bitter taste, while pronase and esp/sav hydrolysate had strong umami taste. From these results, pronase was found to be suitable enzyme for producing file-fish hydrolysate.

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Physicochemical Characteristics of Collagen Peptide from Flatfish Skin (각시가자미 껍질로부터 콜라겐 펩타이드 제조 및 이화학적 특성)

  • Jang, Boo-Sik;Lee, Mi-Jin;Jeong, Noh-Hee;Kim, Tae-Young
    • Applied Chemistry for Engineering
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    • v.24 no.1
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    • pp.18-23
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    • 2013
  • In this research, the collagen peptide powder from flatfish skin (FSCP) was prepared and compared with commercial collagen peptide powder from tilapia scale (TSCP) in the aspect of physiochemical property. The physical property and nutritional components of FSCP appeared almost similarly to those of TSCP, and also in calorie. No differences in calorie between FSCP and TSCP. Amino acid contents of FSCP for example, aspartic acid, serine, histidine, tyrosine and methionine were higher than those of TSCP. In contrast, the hydroxyproline, proline, alanine contents in FSCP were lower than those in TSCP. Especially, the content of essential amino acid of FSCP, which was 22.74%, was higher than that of TSCP evaluated as 13.64%. In the distribution of molecular weight, FSCP was 1000 Da, which showed a comparatively low distribution compared with TSCP, and in emulsion property and stability both FSCP and TSCP showed an excellent trend.

Enhancement of Immune Activities of Peptides from Asterias amurensis Using a Nano-encapsulation Process (나노 입자 불가사리 펩타이드의 면역 활성 증진)

  • Jeong, Hyang-Suk;Oh, Sung-Ho;Kim, Seoung-Seop;Jeong, Myoung-Hoon;Choi, Woon-Yong;Seo, Yong-Chang;Choi, Geun-Pyo;Kim, Jin-Chul;Lee, Hyeon-Yong
    • Korean Journal of Food Science and Technology
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    • v.42 no.4
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    • pp.424-430
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    • 2010
  • Immuno-modulatory activities of peptides from Asterias amurensis were investigated using a nano-encapsulation process. The molecular weights of the peptides in the range of 5-7 kDa were separated using Sephadex G-75 gel filtration. Eighty-five percent of the nano-particles were in the 300 nm range using dynamic light scattering. The cytotoxicity of the A. amurensis nano-particles against CCD-986sk human dermal fibroblast cells was 11.64% after adding 1.0 mg/mL of the samples, which was lower than that from the control (13.28% collagen). The secretion of $NO^-$ from macrophages was estimated as $40\;{\mu}M$ after adding 1.0 mg/mL of gelatin nano-particles, which was higher than the others. Prostaglandin $E_2$ production from UV-induced human skin cells decreased greatly to 860 pg/mL after adding 1.0 mg/mL of the samples. Confocal microscopy revealed that nano-particles effectively penetrated the cells within 1 hour. From these results, we consider that nano-encapsulation of the peptides from A. amurensis can improve their biological functions.