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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.
Antibacterial Activities of Peptides Designed as Hybrids of Antimicrobial Peptides
Shin, Song Yub,Lee, Myung Kyu,Hahm, Kyung Soo,Kang, Joo Hyun 생화학분자생물학회 1982 BMB Reports Vol.29 No.6
CA(1-8)ME(1-12), the CA-ME hybrid peptide of the amino terminal segments of cecropin A (CA) and melittin (ME), has been reported to have a broad spectrum and improved potency without a hemolytic property. In order to obtain new synthetic peptides with powerful antibacterial activity without hemolytic activity, several hybrid peptides were designed from the sequences of CA, ME. magainin 2, bombinin and lactoferricin. All hybrid peptides were constructed to form an amphipathically basic-flexible-hydrophobic structure and synthesized by the solid phase method. Their hemolytic activities against human red blood cells and antibacterial activities against both Gram-positive and Gram-negative bacteria were determined. CA(18)MA(1-12). CA(1-8)BO(1-12). MA(10-17)ME(1-12) and LF(20-29)ME(1-12) showed comparable activities with broad spectra against both Gram-positive and Gram-negative bacteria relative to CA(1-8)ME(1-12) but without hemolytic properties. These hybrid peptides, therefore. could be useful as model peptides to design a novel peptide with improved antibacterial activity and study on structure-activity relationships of antimicrobial peptides.
Shin, Song Yub,Kang, Shin Won,Ha, Jong Myung 생화학분자생물학회 1976 BMB Reports Vol.28 No.2
To investigate the biological functions of the EGF-like domain of mouse betacellulin (BTC), mouse BTC(33-80), a 48-residue peptide corresponding to the EGF-tike domain, was synthesized by stepwise solidphase methods using a 9-fluorenylmethoxycarbonyl (Fmoc) strategy. The homogeneity of synthetic mouse BTC(33-80) was confirmed by analytical reversed phase (RIB-HPLC, amimo acid analysis, and fast atom bombardment mass spectrometer (FA&MS). Three disulfide bond pairings of synthetic mouse BTC(33-80) were established by amino acid analysis of cysteine-containing fragments derived from therrnolytic digestion. These were consistent with the pairings of EGF and hansforming growth factor (TGF-a). The EGF-like domain of mouse BTC showed equipotent activity in both EGF-receptor binding on A-431 epidermoid carcinoma cells, and mitogenesis on NIH-3T3 fibroblast cells, as compared with authentic h-EGF. Results suggest that the EGF-like do=.nain of BTC plays a significant role in mitogenic activity with an EGF-receptor mediated system.
Shin, Song Yub Korean Chemical Society 2014 Bulletin of the Korean Chemical Society Vol.35 No.11
In order to investigate the effects of the double replacement of $\small{L}$-Pro, $\small{D}$-Pro, $\small{D}$-Leu or Nleu (the peptoid residue for Leu) in the hydrophobic face (positions 9 and 13) of amphipathic ${\alpha}$-helical non-cell-selective antimicrobial peptide $L_8K_9W_1$ on the structure, cell selectivity and mechanism of action, we synthesized a series of $L_8K_9W_1$ analogs with double replacement of $\small{L}$-Pro, $\small{D}$-Pro, $\small{D}$-Leu or Nleu in the hydrophobic face of $L_8K_9W_1$. In this study, we have confirmed that the double replacement of $\small{L}$-Pro, $\small{D}$-Pro, or Nleu in the hydrophobic face of $L_8K_9W_1$ let to a great increase in the selectivity toward bacterial cells and a complete destruction of ${\alpha}$-helical structure. Interestingly, $L_8K_9W_1$-$\small{L}$-Pro, $L_8K_9W_1$-$\small{D}$-Pro and $L_8K_9W_1$-Nleu preferentially interacted with negatively charged phospholipids, but unlike $L_8K_9W_1$ and $L_8K_9W_1$-$\small{D}$-Leu, they did not disrupt the integrity of lipid bilayers and depolarize the bacterial cytoplasmic membrane. These results suggested that the mode of action of $L_8K_9W_1$-$\small{L}$-Pro, $L_8K_9W_1$-$\small{D}$-Pro and $L_8K_9W_1$-Nleu involves the intracellular target other than the bacterial membrane. In particular, $L_8K_9W_1$-$\small{L}$-Pro, $L_8K_9W_1$-$\small{D}$-Pro and $L_8K_9W_1$-Nleu had powerful antimicrobial activity (MIC range, 1 to $4{\mu}M$) against methicillin-resistant Staphylococcus aureus (MRSA) and multidrug-resistant Pseudomonas aeruginosa (MDRPA). Taken together, our results suggested that $L_8K_9W_1$-$\small{L}$-Pro, $L_8K_9W_1$-$\small{D}$-Pro and $L_8K_9W_1$-Nleu with great cell selectivity may be promising candidates for novel therapeutic agents, complementing conventional antibiotic therapies to combat pathogenic microorganisms.
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,Lee, Myung-Kyu,Jang, So-Youn,Hahm, Kyung-Soo Korean Society for Biochemistry and Molecular Biol 2000 Journal of biochemistry and molecular biology Vol.33 No.1
The HIV-1 p24(202-221) sequence ETINNEEEWDRVHPV HAGP contains a B-cell epitope with the earliest immune response and the highest antibody titer against anti-mouse sera obtained by immunization with p24 antigens. A novel mouse monoclonal antibody (mAb) was generated against the immunodominant B-cell epitope of the HIV-1 p24 capsid protein, p24(202-221). BALB/c mice were immunized with the four branched multiple antigenic peptide (MAP) containing the HIV-1p24(202-221) sequence, and antibody-secreting hybridoma were produced by fusion of mouse splenocytes with P3X63Ag8.653, mouse myeloma cells. One clone which produced the antigen-specific mAb named KI-24 (Isotype IgG1, light chain: ${\kappa}$) was identified. mAb KI-24 was highly specific for both the p24(202-221) and p24 proteins when analyzed by ELISA and Western blotting. Since p24(202-221) also contains a cytotoxic T-lymphocyte epitope, this specfic peptide epitope and the monoclonal antibody with specific reactivity against the p24 protein and p24(202-221) can be used in peptide vaccine development and p24 antigen detection from HIV patients.