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完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.advisor | 王勝仕(Sheng-Shih Wang) | |
dc.contributor.author | Chih-Yuan Chen | en |
dc.contributor.author | 陳志遠 | zh_TW |
dc.date.accessioned | 2021-06-15T01:39:26Z | - |
dc.date.available | 2012-07-22 | |
dc.date.copyright | 2009-07-22 | |
dc.date.issued | 2009 | |
dc.date.submitted | 2009-07-15 | |
dc.identifier.citation | 1. Arakawa, T., Ejima, D., Tsumoto, K., Ishibashi, M., and Tokunaga, M. (2007) Improved performance of column chromatography by arginine: Dye-affinity chromatography, Protein Expression and Purification 52, 410-414.
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dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/43148 | - |
dc.description.abstract | 精胺酸(L-arginine, L-Arg)為人體內二十種胺基酸之ㄧ,被證實可被用來抑制蛋白質的聚集體。然而,精胺酸對於抑制蛋白質聚集的機制與路徑仍未被了解。此論文中,主要是探討精胺酸對於牛血清蛋白形成聚集體之影響。蛋白質的聚集體大致可分為兩種:不規則性(amorphous)與規則性(amyloid fibril)聚集體。研究發現,精胺酸對於牛血清蛋白的不規則性之聚集體有抑制效果,但對於牛血清蛋白形成之類澱粉纖維卻沒有抑制的效果。探討牛血清蛋白形成類澱粉纖維之作用力,發現精胺酸與牛血清蛋白間有疏水性作用力存在,但卻無法阻止類澱粉纖維形成,只能減緩類澱粉纖維生成之速率;而當牛血清蛋白形成類澱粉纖維的過程中存在三(2-氯乙基)磷酸酯 (TCEP),則有抑制之效果。由此可知,牛血清蛋白應該主要是藉著雙硫鍵形成類澱粉纖維。在某些研究提到,精胺酸對於特定幾種蛋白質的類澱粉纖維有抑制之效果,而這些蛋白質的共通點都是類澱粉纖維主要是藉著疏水或氫鍵作用力而形成。因此,可推測精胺酸只能抑制藉由疏水或氫鍵作用力形成之類澱粉纖維,而無法抑制藉由雙硫鍵形成之類澱粉纖維。 | zh_TW |
dc.description.abstract | L-arginine (L-Arg) which is one of the twenty amino acids in vivo has been demonstrated to exhibit an inhibitory effect against protein aggregation. However, the pathways and mechanism of the aggregate suppression by L-Arg remain largely unknown. In this research, attempts were directed toward examining the influence of L-Arg on the aggregated species of bovine serum albumin (BSA). The BSA aggregates can be generally divided into two groups: disordered (amorphous) and ordered (amyloid fibril) aggregates. We first explored how BSA was converted into amyloid fibril and then found that hydrophobic interaction exists between BSA and L-Arg. Furthermore, our data revealed that L-Arg could inhibit the formation of disordered BSA aggregate but not prevent amyloid fibril. Besides, the addition of reducing agent TCEP led to an inhibition of BSA amyloid fibrils, suggestive of the key role of disulfide bonds in forming BSA amyloid fibrils. Findings from previous studies indicated that L-Arg possesses an inhibitory potency against the formation of amyloid fibrils which is mainly governed by the hydrophobic interaction or hydrogen bonding. Therefore, along with our results, we can conjecture that L-Arg probably can not inhibit the amyloid fibrillation associated with disulfide bonds. | en |
dc.description.provenance | Made available in DSpace on 2021-06-15T01:39:26Z (GMT). No. of bitstreams: 1 ntu-98-R96524086-1.pdf: 19226212 bytes, checksum: c921aad7fee30198f53a5337243da562 (MD5) Previous issue date: 2009 | en |
dc.description.tableofcontents | 摘要 I
Abstract II 目錄 III 圖目錄 XII 表目錄 XIII 第一章 緒論 1 第二章 文獻回顧 2 2-1 類澱粉症(amyloidosis) 2 2-2 蛋白質介紹 4 2-2-1 一級結構 6 2-2-2 二級結構 6 2-2-3 三級結構 8 2-2-4 四級結構 9 2-3蛋白質的摺疊 10 2-3-1蛋白質的摺疊原理 10 2-3-2 蛋白質的構形 11 2-3-3 蛋白質結構間的作用力 12 2-2-3-1胜肽鍵 12 2-2-3-2雙硫鍵 12 2-2-3-3氫鍵 13 2-2-3-4 離子作用力 13 2-2-3-5疏水性作用力 13 2-4蛋白質的聚集 14 2-4-1聚集體的形成 15 2-4-2 聚集體的構造 17 2-5蛋白質的雙硫鍵 21 2-5-1蛋白質雙硫鍵的生成 21 2-5-2蛋白質雙硫鍵的斷裂 22 2-6 血清蛋白(Serum albumin) 23 2-6-1牛血清蛋白(Bovine serum albumin, BSA)之介紹 24 2-6-2牛血清蛋白形成聚集體之介紹 28 2-7 精胺酸(L-arginine) 32 2-8 蛋白質聚集之測量方法 38 2-8-1 ThT螢光放射 38 2-8-2 剛果紅鍵結 39 2-8-3 ANS螢光測試 40 2-8-4 圓二色光譜分析 41 2-8-5 蛋白質濃度測定 43 第三章 研究動機 45 第四章 實驗裝置、藥品與步驟 46 4-1實驗儀器 46 4-2 實驗藥品 47 4-3 實驗步驟 49 4-3-1精胺酸溶液配置 49 4-3-2 BCA蛋白質濃度分析(BCA assay) 49 4-3-3蛋白質樣品製備 49 4-3-4移除精胺酸 50 4-3-5 ThT螢光光譜分析(Thioflavin T fluorescence spectroscopy) 50 4-3-6 剛果紅染劑鍵結分析(Congo red biding assay) 50 4-3-7 ANS螢光光譜分析(ANS fluorescence spectrometry) 51 4-3-8 遠紫外光圓二色光譜分析(Far-UV CD spectroscopy) 51 4-3-9 穿透式電子顯微鏡(Transmission electron microscopy, TEM) 52 4-3-10蛋白質之濁度測定 52 4-3-11自身螢光光譜分析法(Intrinsic fluorescence spectrometry) 52 4-3-12蛋白質樣品添加TCEP之製備 52 4-3-13蛋白質電泳(Protein gel electorphoresis) 53 4-3-13-1 製做SDS-PAGE膠片 53 4-3-13-2 蛋白質電泳實驗 53 4-3-14 動態光散射分析 (Dynamic Light Scattering) 55 第五章 實驗結果與討論 56 5-1 精胺酸對牛血清蛋白聚集體之影響 56 5-1-1 精胺酸對牛血清蛋白形成不規則性聚集體之影響 56 5-1-2 利用高溫誘導牛血清蛋白形成類澱粉纖維 58 5-1-3 精胺酸對牛血清蛋白形成類澱粉纖維之影響 61 5-1-4 探討牛血清蛋白形成類澱粉纖維疏水性區域之變化 65 5-1-5 穿透式電子顯微鏡(TEM)分析類澱粉纖維 67 5-1-6 動態光散射(DLS)分析牛血清蛋白之聚集現象 69 5-2 精胺酸影響ThT染劑與類澱粉纖維的結合 72 5-3 探討移除精胺酸後各項實驗之結果 75 5-3-1 移除精胺酸後精胺酸對牛血清蛋白形成類澱粉纖維之影響 75 5-3-2 移除精胺酸後探討牛血清蛋白形成類澱粉纖維疏水性區域之變化 78 5-3-3 移除精胺酸後探討牛血清蛋白形成類澱粉纖維自身螢光之變化 79 5-3-4探討精胺酸對牛血清蛋白二級結構之影響 82 5-3-5牛血清蛋白之電泳分析 86 5-4探討精胺酸為何無法抑制牛血清蛋白形成類澱粉纖維 88 5-4-1 牛血清蛋白與精胺酸之間的作用力 88 5-4-2 假設牛血清蛋白之類澱粉纖維藉由疏水性及氫鍵作用力形成 90 5-4-3 假設牛血清蛋白之類澱粉纖維藉由雙硫鍵鍵結形成 98 5-4-4牛血清蛋白與TCEP之電泳分析結果 101 5-4-5 調整pH值後TCEP對牛血清蛋白之影響 105 5-5實驗結果整理 108 第六章 結論與建議 109 6-1精胺酸對於牛血清蛋白的不可溶性聚集體之影響 109 6-2精胺酸對於牛血清蛋白的類澱粉纖維之影響 109 6-3牛血清蛋白形成類澱粉纖維之機制 110 6-4總結 114 參考文獻 115 附錄 124 附錄A牛血清蛋白濃度之校正曲線 124 附錄B牛血清蛋白離心前後二級結構之變化 125 附錄C不同蛋白質的聚集體抑制劑對牛血清蛋白形成類澱粉纖維之影響 126 附錄D蛋白質電泳實驗對於有無添加β-ME之影響 130 附錄E牛血清蛋白之類澱粉纖維生成動力學 131 | |
dc.language.iso | zh-TW | |
dc.title | 研究精胺酸與牛血清蛋白的聚集體之交互作用 | zh_TW |
dc.title | Research of the Interaction Between L-Arginine and Bovine Serum Albumin Aggregates | en |
dc.type | Thesis | |
dc.date.schoolyear | 97-2 | |
dc.description.degree | 碩士 | |
dc.contributor.oralexamcommittee | 王孟菊(Meng-Jiy Wang),侯劭毅(Shao-Yi Hou),林達顯(Ta-Hsien Lin) | |
dc.subject.keyword | 類澱粉纖維,牛血清蛋白,精胺酸,還原劑,聚集體,雙硫鍵,TCEP, | zh_TW |
dc.subject.keyword | amyloid fibril,BSA,L-arginine,reducing agent,aggregates,disulfide bond,TCEP, | en |
dc.relation.page | 134 | |
dc.rights.note | 有償授權 | |
dc.date.accepted | 2009-07-15 | |
dc.contributor.author-college | 工學院 | zh_TW |
dc.contributor.author-dept | 化學工程學研究所 | zh_TW |
顯示於系所單位: | 化學工程學系 |
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