• Title/Summary/Keyword: Melittin-related peptide

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RV-23, a Melittin-Related Peptide with Cell-Selective Antibacterial Activity and High Hemocompatibility

  • Zhang, Shi-Kun;Ma, Qian;Li, Su-Bo;Gao, Hong-Wei;Tan, Ying-Xia;Gong, Feng;Ji, Shou-Ping
    • Journal of Microbiology and Biotechnology
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    • v.26 no.6
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    • pp.1046-1056
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    • 2016
  • RV-23 is a melittin-related antibacterial peptide (MRP) with lower cytotoxicity than either melittin or AR-23, another MRP. The aim of this study was to explore the mechanism of RV-23's antibacterial selectivity and its hemocompatibility. The results showed that all the peptides exhibited lytic activity against Staphylococcus aureus and Escherichia coli, with RV-23 showing the highest potency. Moreover, RV-23 had lower cytotoxicity than melittin or AR-23 at their minimal inhibitory concentration. In addition, CD experiments showed that melittin, RV-23, and AR-23 all had a typical α-helical structure, and RV-23 had the lowest α-helix content. The structural information showed that RV-23 has the lowest hydrophobicity and highest hydrophobic moment. Because hydrophobicity and α-helix content are believed to correlate with hemolysis, the results indicate that the selective lytic activity against bacteria of RV-23 may be due to its low hydrophobicity and α-helicity, which lead to low cytotoxicity without affecting antibacterial activity. Furthermore, RV-23 did not affect the structure and function of blood components such as red blood cells, platelets, albumin, and the blood coagulation system. In conclusion, RV-23 is a cell-selective antibacterial peptide with high hemocompatibility due to its unique structure.

cDNA microarray gene expression profiling of melittin and mast cell degranulation peptide in human mast cell strain (봉독의 주요성분인 Melittin과 MCDP이 비만세포주에서 유전자 발현에 미치는 영향에 대한 microarray 분석)

  • So, Jae-jin;Woo, Hyun-su;Kim, Chang-hwan
    • Journal of Acupuncture Research
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    • v.22 no.3
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    • pp.37-51
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    • 2005
  • Mast cell is a cell that functions mainly in our body with a respect to inflammation and allergic response. Bee venom has been progressed in a study as a model related to mechanism in alleviation of pain until now, but it is being progressed in a study relevant to immunocyte in anti-inflammation or anti-allergic response. The present study is aimed to present the basis related to a future study of gene, by researching the influence of melittin and MCD Peptide, which are major ingredients in Bee venom, upon the expression of gene in the mast cell strain. In this study, it dealt with melittin and MCD Peptide respectively, in the effective concentration after passing though the experiment of cytotoxicity by using human mast cell strain. Also, with the respect in the aspect of expression in gene that changes at this time, information was obtained through the technique of analyzing microarray. Through experimental statistics, when regarding a case that global M is significant in more than 1 or -1, in melittin, all 7 genes were accelerated, and 8 inhibited. In MCDP, 7 genes were accelerated and 17 genes inhibited. The function in the body to which these genes are related, was associated with the protein binding within a cell, the activation in the function of lymphocyte, the acceptor related to macrophage antigen. In cell nucleus, substance related to GABA A receptor, protein associated with cAMP reactive element, substance related to complement system No.8 and to B-cell, protein substance related to polycystic kidney disease, substance related to inflammation, and the protein substance of influencing coagulation of blood. Through these results of analysis, it could obtain more useful materials in clarifying the mechanism of action in melittin and MCD peptide, which are in charge of mainly medical action in the abdomen. Also, it is thought that an in-depth study on the influence of main ingredients in Bee venom, the wholly honey bee venom aqua upon anti-allergic response or anti-inflammation are further required.

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The Review on the Study related to Anti-inflammatory Mechanism of Bee Venom Therapy (봉독요법(蜂毒療法)의 항염증(抗炎症) 기전(機轉) 연구(硏究)에 관(關)한 고찰(考察))

  • Choi, Jung-Sik;Park, Jang-Woo;Oh, Min-Seok
    • Journal of Haehwa Medicine
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    • v.15 no.1
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    • pp.141-160
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    • 2006
  • The obtained results are summarized as follows 1. New findings are reporting year by year as for the study related to Anti-inflammatory mechanism of Bee Venom therapy. 2. The Anti-inflammatory effect of Bee Venom therapy is achieved through counterirritation, stimulations to adrenal cortex, immuno-regulation, antioxidation, removal of free radicals, modulation of AGP gene induction. 3. The chief components of Bee Venom related to Anti-inflammatory effect are Melittin, MCD peptide, Apamin, Adolapin etc. 4. Melittin binds to secretory phospholipase A2 and inhibits its enzymatic activity. 5. Melittin blocks neutophil O2-production. 6. MCD peptide(Peptide 401) stimulates the mast cell secrets histamine, Anti-inflammatory effect caused by this is 'conterirritation'. 7. Melittin & Apamin have an anti-inflammatory effect by inducing cortisone secretion. 8. MCD peptide & Apamin increase immunologic fuction by stimulating hypophysis & adrenal cortex and have an anti-inflammatory effect by inhibiting synthesis of prostaglandin from arachidonic acid. 9. Adolapin have an anti-inflammatory effect by inhibiting COX. 10. Bee Venom have an anti-inflammatory effect by suppressing AGP($\alpha$-acid glycoprotein). 11. Bee Venom have an anti-inflammatory effect by inhibiting NO, iNOS, PLA2, COX-2, TNF-$\alpha$, IL-1, NF-${\kappa}B$, MAP kinase.

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Systemic Review: The Study on Bee Venom Related to Cancer in PubMed (암관련 봉독 연구에 대한 고찰-PubMed를 이용한 Medline 검색)

  • Yun, Hyoun-Seok;Lee, Jae-Dong;Lee, Yun-Ho
    • Journal of Acupuncture Research
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    • v.17 no.4
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    • pp.69-78
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    • 2000
  • Objective : To research the trends of the study related to bee venom and cancer, and to establish the hereafter direction of the study on bee venom herbal acupuncture. Method : We searched in PubMed, with bee venom and cancer(in English, with abstract) Results : 1. We searched 28 Journals, 36 Papers. the frequency of Journals and Papers was as follows: Biochem Biophys Res Commun(4 Papers), FEBS Lett(3), Life Sci, Proc Natl Acad Sci USA, J Immunol(each 2), other 23 Journals(each 1). 2. The pattern of the study was as follows: Review article(3 Journals, 3 Papers), Epidemiologic study(1, 1), Experimental study(24, 32) In vivo 1, 1), In vitto(24, 31) 3. The involved components of bee venom were as follows: Melittin(20), Apamin(8), Phospholipase A2(3), Melittin & Phospholipase A2(3), Melittin& Tertiapin(1). 4. The involved cancer was as follows: leukemia(9), tumor(5), neuroblastoma(4), pituitary tumor and pheochromocytoma(each 3), lymphoma, astrocytoma, glioma and lung cancer(small cell carcinoma)(eacn 2), bladder carcinoma, pancreatic cancer, breast carcinoma, ovarian carcinoma and spuamous cell carcinoma(each 1) Conclusion : We concluded that the most frequent pattern of the study was in vitro experimental study with peptide components of bee venom and the most frequeni invovled cancer was leukemia.

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Antifungal activities of peptides with the sequence 10-17 of magainin 2 at the N-termini against aspergillus fumigatus (Antifungal Activities of Peptides with the Sequence 10-17 of Magainin 2 at the N-termini against Aspergillus fumigatus)

  • Lee, Myung Kyu;Lee, Dong Gun;Shin Song Yub;Lee, Sung Gu;Kang Joo Hyun;Hahm, Kyung Soo
    • Journal of Microbiology
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    • v.34 no.3
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    • pp.274-278
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    • 1996
  • Two peptides, MA-inv AND MA-ME, with the sequence 10-17 of maganin 2 at their-N-termini were designed and synthesized. The peptides had higher antifungal activities against Aspergilus fumigatus without hemolytic activities. The minimal inhibition concentratory (MIC) values of both peptides against A. fumigatus were 5 .mu.g/ml, whereas those of the native peptides, magainin 2 and melittin, were 10.mu.g/ml. At 3 .mu.g/ml, MA-inv and MA-ME inhibited the mycelium growth of A. fumigatus by 94.6% and 97.3% respectively, whereas magainin 2 and melittin inhibited by 62.2% and 32.4, respectively. MA-inv showed up to 80% inhibition of (1, 3)-.betha.-D-glucan synthase activity of A. fumigatus. The peptides also showed up to 80% inhibition of (1, 3)-.betha.-D glucan synthase activity of A. fumigatus. The peptides also showed antifungal activities for other fungi of Aspergillus sp. However, the antibiotic activities of MA-ME against Escherichia coli, Bacillus subtilis and Fusarium oxysporum were more effective than those of MA-inv, suggesting that the C-terminal sequences of MA-inv and MA-ME may also influence their antibiotic activities. These results suggest that the N-terminal sequence of the designed peptides, KKFGKAFV, is important for their antifungal activities against A. fumigatus and their C- terminal sequences are related to the organism selectivity.

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