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http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/95724完整後設資料紀錄
| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 陳振中 | zh_TW |
| dc.contributor.advisor | Jerry Chun Chung Chan | en |
| dc.contributor.author | 李夏安 | zh_TW |
| dc.contributor.author | Hsia-An Lee | en |
| dc.date.accessioned | 2024-09-15T17:00:34Z | - |
| dc.date.available | 2024-09-16 | - |
| dc.date.copyright | 2024-09-15 | - |
| dc.date.issued | 2024 | - |
| dc.date.submitted | 2024-08-12 | - |
| dc.identifier.citation | Prusiner, S. B. A Unifying Role for Prions in Neurodegenerative Diseases. Science. 2012, 336 (6088), 1511–1513.
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K.; Schiene-Fischer, C.; Fändrich, M.; Grigorieff, N. Peptide Dimer Structure in an Aβ(1–42) Fibril Visualized with Cryo-EM. Proc. Natl. Acad. Sci. 2015, 112 (38), 11858–11863. Gremer, L.; Schölzel, D.; Schenk, C.; Reinartz, E.; Labahn, J.; Ravelli, R. B. G.; Tusche, M.; Lopez-Iglesias, C.; Hoyer, W.; Heise, H.; Willbold, D.; Schröder, G. F. Fibril Structure of Amyloid-β(1-42) by Cryo-Electron Microscopy. Science. 2017, 358 (6359), 116–119. | - |
| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/95724 | - |
| dc.description.abstract | 普里昂蛋白 (PrP) 是引發人類庫賈氏症、狂牛症以及羊搔癢症的主要蛋白質，其異常折疊造成腦組織空洞化。先前的研究指出，普里昂蛋白為乙型類澱粉蛋白 42 (Aβ42) 寡聚物具高親和性的受體。此外，PrP 與 Aβ42 寡聚物的結合被認為與阿茲海默症的惡化過程有密切相關性。為了探討 PrP 與 Aβ42 的相互作用，本研究運用直徑平均為 28 nm 的逆相微胞來共培養 PrP 和 Aβ42 單體，並使用動態光散射儀確認逆相微胞的大小，以及利用硫磺素 T 螢光檢測法和穿透式電子顯微鏡探討在共培養的條件下 PrP 和 Aβ42 能否產生共寡聚物。實驗結果顯示，逆相微胞中的限制性物理空間能增加 PrP 與 Aβ42 寡聚物的相互作用，比單獨培養PrP時形成較多 β-sheet 的結構。本研究進一步使用原子力顯微鏡來量測 PrP、Aβ42 以及共培養 PrP—Aβ42 纖維的高度及硬度值，結果顯示三者的硬度值在統計上並沒有顯著的差異。 | zh_TW |
| dc.description.abstract | Prion protein (PrP) is the culprit that causes human Creutzfeldt-Jakob disease, mad cow disease and scrapie in sheep. Its abnormal folding causes the spongy form of brain tissues in patients. Previous studies have shown that PrP is a high-affinity receptor for the oligomers of beta amyloid 42 peptides (Aβ42). Moreover, the binding between PrP and Aβ42 oligomers is closely associated to the progression of Alzheimer's disease. In order to investigate the interaction between PrP and Aβ42, this study used reverse micelles (RM) with an average diameter of 28 nm to co-incubate PrP and Aβ42 monomers. The size of RM was monitored by dynamic light scattering (DLS), and the interaction between PrP and Aβ42 was investigated by Thioflavin-T (ThT) assay and transmission electron microscopy (TEM). The results showed that the confined physical space of the RM can enhance the binding of PrP and Aβ42 oligomers. The resultant PrP–Aβ42 aggregates had more β-sheet structure than the aggregates formed by PrP alone. We then used atomic force microscopy (AFM) to measure the height and Young’s modulus of the fibrils of PrP, Aβ42 and PrP–Aβ42. The results indicate that the Young's modulus of the three types of fibrils have no significant difference. | en |
| dc.description.provenance | Submitted by admin ntu (admin@lib.ntu.edu.tw) on 2024-09-15T17:00:34Z No. of bitstreams: 0 | en |
| dc.description.provenance | Made available in DSpace on 2024-09-15T17:00:34Z (GMT). No. of bitstreams: 0 | en |
| dc.description.tableofcontents | 謝誌 II
中文摘要 VI Abstract VII 縮寫表 VIII 目次 XI 圖次 XIV 表次 XIX 第一章 緒論 1 1.1 神經退化性疾病與致病蛋白的聚集 1 1.1.1 普里昂蛋白在神經退化性疾病的關鍵作用與傳播機制 3 1.1.2 普里昂蛋白與乙型類澱粉蛋白的關係 6 1.2 普里昂蛋白 7 1.2.1 結構與功能 7 1.2.2 錯誤折疊與轉化機制 10 1.3 乙型類澱粉蛋白 14 1.3.1 胜肽的形成與聚集 15 1.3.2 寡聚物與致病機制 17 1.4 普里昂蛋白與乙型類澱粉蛋白 42 的相互作用 21 1.5 逆相微胞系統 25 1.6 研究動機 29 第二章 實驗方法及鑑定技術 30 2.1 化學藥品與儀器 30 2.2 蛋白製備 34 2.2.1 普里昂蛋白 35 2.2.2 乙型類澱粉蛋白 41 2.3 蛋白鑑定 46 2.3.1 電噴灑游離法質譜儀 46 2.3.2 基質輔助雷射脫附游離/飛行時間式質譜儀 47 2.4 樣品製備 49 2.4.1 PrP 單體製備 49 2.4.2 Aβ42 單體製備 49 2.4.3 使用逆相微胞製備共聚物 50 2.4.4 反向萃取蛋白共聚物 50 2.5 鑑定技術 51 2.5.1 動態光散射粒徑分析儀 51 2.5.2 硫磺素 T 螢光檢測法 52 2.5.3 斑點印跡法 53 2.5.4 穿透式電子顯微鏡 55 2.5.5 原子力顯微鏡 57 2.5.5.1 基本原理 57 2.5.5.2 實驗使用之設備與物件 62 2.5.5.3 樣品製備 66 2.5.5.4 恆定力輕敲式掃描模式 67 2.5.5.5 定量材料性質之曲線分析 69 第三章 類澱粉樣蛋白的自聚集與共培養 74 3.1 蛋白純化與鑑定 74 3.1.1 PrP 74 3.1.2 Aβ42 75 3.2 單體自聚集纖維化的測試 77 3.2.1 PrP 77 3.2.2 Aβ42 79 3.3 逆相微胞製備寡聚物與性質鑑定 81 3.3.1 RM-(PrP) 81 3.3.2 RM-(Aβ42) 85 3.3.3 RM-(Aβ42)/(PrP) 87 3.3.4 類澱粉樣纖維的結構特徵和機械性質量測 90 3.4 逆相微胞作 PrP 與 Aβ42 共培養的系統 95 3.4.1 pH 值的影響 95 3.4.2 Aβ42 濃度的影響 96 3.4.3 空間限制的影響 99 3.5 章節總結 101 第四章 結論與未來展望 102 4.1 論文總結 102 4.2 未來展望 103 參考文獻 104 附錄 115 附錄 A 鹽類濃度與 pH 值對 PrP 單體自聚集的影響 115 附錄 B Aβ42 HPLC 標準曲線 119 附錄 C Aβ42 於不同環境下的濃度測試 121 附錄 D PrP, Aβ42, PrP–Aβ42 於不同擬合範圍的硬度值分析 123 | - |
| dc.language.iso | zh_TW | - |
| dc.title | 利用原子力顯微鏡測量老鼠普里昂蛋白與乙型類澱粉蛋白 42 共培養之類澱粉樣纖維 | zh_TW |
| dc.title | Characterization of Co-Incubated Amyloid Fibrils of Mouse Prion Protein and Beta Amyloid Peptide 42 by Atomic Force Microscopy | en |
| dc.type | Thesis | - |
| dc.date.schoolyear | 112-2 | - |
| dc.description.degree | 碩士 | - |
| dc.contributor.oralexamcommittee | 黃英碩;陳佩燁;黃人則 | zh_TW |
| dc.contributor.oralexamcommittee | Ing-Shouh Hwang ;Rita Pei-Yeh Chen;Joseph Jen-Tse Huang | en |
| dc.subject.keyword | 普里昂蛋白,乙型類澱粉蛋白,逆相微胞,寡聚物,原子力顯微鏡, | zh_TW |
| dc.subject.keyword | prion protein,beta-amyloid,reverse micelles,oligomers,atomic force microscopy, | en |
| dc.relation.page | 132 | - |
| dc.identifier.doi | 10.6342/NTU202404166 | - |
| dc.rights.note | 同意授權(全球公開) | - |
| dc.date.accepted | 2024-08-13 | - |
| dc.contributor.author-college | 理學院 | - |
| dc.contributor.author-dept | 化學系 | - |
| dc.date.embargo-lift | 2029-08-09 | - |
| 顯示於系所單位： | 化學系 | |
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