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    Please use this identifier to cite or link to this item: http://tkuir.lib.tku.edu.tw:8080/dspace/handle/987654321/93994

    Title: Mastoparan-B及其衍生物在TFE與SDS環境下結構、動力學的行為與活性的關係
    Other Titles: Relationship between structure, backbone dynamics and activity of Mastoparan-B and its analogues in TFE and SDS environment
    Authors: 張鴻鈞;Jhang, Hong-Jyun
    Contributors: 淡江大學化學學系碩士班
    李長欣;Lee, Chang-Shin
    Keywords: 抗菌胜肽;核磁共振;動力學;化學位移;NMR;13C relaxation;dynamics;diffusion;Antimicrobial peptides;Model-Free
    Date: 2013
    Issue Date: 2014-01-23 13:46:15 (UTC+8)
    Abstract: Mastoparan B (MPB-NH2)從胡蜂毒液分離出的抗菌胜肽,由14 個
    獻指出2 號位置的lysine 與九號位置的tryptophan 對MPB-NH2 有重
    要的影響。我們分別用asparagine 與tyrosine 置換上述殘基,形成
    Y9-MPB-NH2 及N2Y9-MPB-NH2 的MPB-NH2 衍生物,並使用SDS
    與TFE 兩種不同溶液環境在溫度310 K 來探討MPB-NH2 與其衍生物
    MPB-NH2 與N2Y9-MPB-NH2。CD 實驗觀察到MPB-NH2 及其衍生物
    在水中為無序纏繞的構形,在30 % TFE 溶液中與SDS 微胞中形成α
    螺旋結構。但在SDS 微胞中,MPB-NH2 與Y9-MPB-NH2 的α 螺旋含
    量均比在30 % TFE 溶液中來得高。從Model-free 分析MPB 胜肽在
    TFE 水溶液的動力學行為發現,N2Y9-MPB-NH2 在N 端的動性較另
    外兩條胜肽穩定。擴散實驗表示Y9-MPB-NH2 與N2Y9-MPB-NH2 在
    TFE 310 K 具有相似的寡聚現象,這兩條胜肽分子間相互作用的能量
    也相似。再比較在TFE 與SDS 環境改變時胜肽的化學位移變化,我
    們觀察到Y9-MPB-NH2 與N2Y9-MPB-NH2 的N端NH化學位移有不
    同的表現,可能是N 端電荷與膜作用改變所導致。
    MPB 抑菌活性的表現受到N 端與C 端的正電荷Lys 殘基與膜結
    合能力的影響,動性較大的N 端在與膜結合時,誘發N 端helix 的形
    Mastoparan B (MPB) is an antimicrobial peptide that was isolated from the hornet
    (Vespa basalis) venom. It’s composed of 14 amino acids, containing multiple positive
    charge residues and amidated C-terminus. Studies have suggested that the lysine at position
    2 and the tryptophan at position 9 are important for the activities of MPB. To probe
    their role for structure and activity, we synthesized three peptides, MPB, Y9 (mutated at
    position 2 with asparagines) and N2Y9 (mutated at position 2 and 9 with asparagines and
    tyrosine, respectively). We investigated their antimicrobial activity, structure and dynamics
    at 310 K in both 30%/70% TFE/H2O and SDS micell solutions.
    Antimicrobial activity of the peptides, in sequence from the highest to the lowest, is
    showed as MPB, Y9 and N2Y9. Circular dichroism (CD) spectra indicated that the peptides
    adopt random coil conformation in water and α-helical structure in TFE and SDS
    micell solutions. In TFE, the N-terminal structures of MPB and Y9 are demonstrated more
    diverged and flexible than that of N2Y9. However, MPB and Y9 form longer and more
    stable helical structures in SDS environment. It is suggested that the affinity of binding
    with SDS for MPB and Y9 is higher than for N2Y9. The diffusion studies showed that the
    oligomerized behaviors of Y9 and N2Y9 are similar in TFE. It indicates that these two
    peptides with similar energetics in intermolecular interactions. As changed from TFE to
    SDS environment, the change profile of NH chemical shifts in N-terminal is quite different
    between Y9 and N2Y9.It may contribute to the consequence of N-terminal charge
    interacted with membrane.
    Antibacterial activity of MPB and its binding ability with membrane are affected by
    the positive charge residue Lys at N-terminal and C-terminal. The flexible N-terminal
    when contact with membrane will form active conformation to facilitate the insertion of
    hydrophobic residues into membrane. Trp as well as the hydrophobic residues on one side
    of the amphipathic helix can affect the capacity of peptide into hydrophobic membrane
    Appears in Collections:[化學學系暨研究所] 學位論文

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