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Melittin-Hybrid 합성 폡타이드가 Fusarium oxysporum의 성장에 미치는 저해효과
이동건,신송엽,이성구,이명규,함경수 한국미생물생명공학회 ( 구 한국산업미생물학회 ) 1996 한국미생물·생명공학회지 Vol.24 No.5
꿀벌의 독액으로부터 분리된 ME은 강항 항균활성을 가지나, 진핵세포에 대하여 세포독성 활성을 포함하고 있다. 본 연구에서는 구조와 항진균활성과 상관관계를 검토하며, 세포독성을 가지지 않으며 보다 강한 항진균활성을 가진 펩타이드의 디자인하기 위하여, ME와 CA 또는 MA으로 이루어진 hybid 펩타이드인 MA(10-17)ME(1-12) 및 CA(1-8)ME(1-12)을 고상합성법의 의하여 합성 하였다. CA(1-8)ME(1-12) 및 MA(10-17)ME(1-12)는 인간의 적혈구에 대하여 용혈현상을 나타내지 않으며, Fusarium oxysporum에 대하여 ME 만큼의 강한 항진균활성을 나타내었다. 또한 이들 hybrid 펩타이드는 (1,3)-β-D-glucan synthase의 활성을 강하게 억제하였다. 이 결과는 Fusarium oxysporum에 대한 hybrid 펩타이드의 활성은 균의 세포벽의 합성의 억제에 의한 것과 관련성이 있는 것을 시사한다. 또한 본 연구의 결과는 세포독성을 가지며 강한 항진균활성을 가지는 펩타이드의 설계에 기초를 제공하였다고 생각된다. 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 inhibition of (1,3)-β-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.
SHIN, SONG YUB,KANG, JOO HYUN,LEE, DONG GUN,JIN, ZHE ZHU,JANG, SO YOUN,KIM, KIL LYONG,HAHM, KYUNG-SOO 한국미생물 · 생명공학회 1999 Journal of microbiology and biotechnology Vol.9 No.3
In order to determine the functional region of the antifungal protein (AFP) isolated from Aspergillus giganteus responsible for growth inhibitory activity and the promotion of phospholipid vesicle aggregation, overlapping peptides covering the complete sequence of AFP were synthesized. The antibiotic activity against bacterial, fungal, and tumor cells, and the vesicle-aggregation activity of the synthetic peptides were investigated. The AFP functional sequence responsible for antibiotic and vesicle-aggregation activity was determined to be located within the region between AFP residues 19 to 32. AFP (19-32) exhibited an α-helical conformation in a cell membrane-like environment. AFP (19-32) displayed potent antibiotic activity against bacterial, fungal, and tumor cells without peptide toxicity as indicated by hemolysis. Accordingly, AFP (19-32) could be used as a good model for the design of effective antibiotic agents with powerful antibiotic activity yet without any cytotoxic effects against the host organism.
Structure-Antifungel Activity Relationships of Cecropin A Hybrid Peptides against Trichoderma sp.
Shin, Song-Yub,Lee, Dong-Gun,Lee, Sung-Gu,Kim, Kil-Lyong,Lee, Myung-Kyu,Hahm, Kyung-Soo The Microbiological Society of Korea 1997 The journal of microbiology Vol.35 No.1
The hybrid peptides, CA-ME, CA-MA and CA-BO, with the N-terminal sequence 1-8 of cecropin A and the N-terminal sequences 1-12 of melittin, magainin 2 and bombinin, respectively, have more improved antibacterial activities. CA-MA was found to have stronger antifungal activity against Trichoderma sp than other hybrid peptides and their parental peptides. In order to elucidate the relationships between the peptide structure and antifungal activity, several analogues of CA-MA or CA-BO were also designed and synthesized by the solid phase method. An tifungal activity was measured against T. reesei and T. viride, and hemolytic activity was measured by a solution method against human red blood cells. The residue 16 of CA-MA, Ser, was found to be important for antifungal activity. When the residue was substituted with Leu, showed powerful antifungal activity was dramatically decreased. CA-MA, P1, P4 and P5 designed in this study showed powerful antifungal activity against T. reesei and T. viride with low hemolytic activity against human red blood cells. These hybrid peptides will be potentially useful model to further design peptides with powerful antifungal activity for the effective therepy of fungal infection and understand the mechanisms of antifungal actions of hybrid peptides.
Shin, Song-Yub,Park, Jung-Hyun,Jang, So-Youn,Lee, Myung-Kyu,Hahm, Kyung-Soo Korean Society for Biochemistry and Molecular Biol 1998 Journal of biochemistry and molecular biology Vol.31 No.1
In this study, a mouse monoclonal antibody (mAb) against gp41(584-618), the immunodominant epitope protein, was generated. For this purpose, BALB/c mice were immunized with double branched multiple antigenic peptides derived from the HIV-1 gp41(584-618) sequence, and antibody-secreting hybridoma were produced by fusion of mice splenocytes with SP2/0 myeloma cells. One clone producing an antigen specific mAb, termed KI-41(isotype IgG1) was identified, whose specific reactivity against gp41(584-618) could be confirmed by ELISA and Western blot analysis. Epitope mapping revealed the recognition site of the mAb KI-41 to be located around the sequence RILAVERYLKDQQLLG, which comprises the N-terminal region within the immunized gp41(584-618) peptied. Since this mAb recognizes this specific epitope within the HIV-1 gp41 without any cross-reactivity to other immunodominant regions in the HIV-2 gp35, KI-41 will provide some alternative possibilities in further applications such as the development of indirect or competitive ELISA for specific antibody detection in HIV-1 infection or for other basic researches regarding the role and function of HIV-1 gp41.