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    Please use this identifier to cite or link to this item: http://ir.lib.ncu.edu.tw/handle/987654321/68107

    Title: 利用籠化TDP-43胜肽片段觀察光引導類澱粉纖維形成之過程;Monitoring the light-induced amyliodogenesis with caged TDP-43 peptides
    Authors: 趙書漢;Chao,Shu-Han
    Contributors: 化學學系
    Keywords: 胜肽;TDP-43
    Date: 2015-07-20
    Issue Date: 2015-09-23 10:44:55 (UTC+8)
    Publisher: 國立中央大學
    Abstract: 透過實驗室先前的研究成果,我們發現TDP-43 蛋白質的胜肽片
    AICAR 後mislocalization 的TDP-43 蛋白質相互作用。透過足夠UV
    TDP-43 蛋白質互相作用,並經由引晶效應(seeding effect)使TDP-43
    ALS 在疾病上的模型(disease model),且可以期待它在其它神經退
    化性疾病中的廣泛討論與應用。;Photolytic device has been used widely in the controlled release of
    chemicals. Previously we have identified the core sequence of TDP-43’s
    C terminus and characterized its rapid aggregation and amyloidogenesis.
    In this study, we synthesized a photochemically inducible peptide.
    Provided that the amyloidogenicity of the peptide would be only activated
    upon UV-initiated photocleavage. From 1) the ultrastructural changes
    observed under a transmission electron microscope (TEM), 2) the
    secondary structure alteration revealed by circular dichroism (CD), and 3)
    the turbidity assessed by UV–visible spectrophotometer, the significant
    changes of the peptide after UV illumination were reported. In addition to
    the in vitro characterizations, the fluorophore was conjugated to the
    peptide to learn its dynamics in neuronal cells since it also confers cell
    membrane permeability. Of note, only UV-mediated release of this
    peptide is capable of triggering cytosolic TDP-43 to form amyloid fiber.
    Taken these together, this photochemically inducible peptide could serve
    as a simple but powerful disease model of ALS and its further application
    on neurodegenerative diseases is highly expected as well.
    Appears in Collections:[化學研究所] 博碩士論文

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