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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 | Pu Wang | en |
dc.contributor.author | 王卜 | zh_TW |
dc.date.accessioned | 2021-06-13T15:33:57Z | - |
dc.date.available | 2013-07-17 | |
dc.date.copyright | 2008-07-17 | |
dc.date.issued | 2008 | |
dc.date.submitted | 2008-07-11 | |
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dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/37589 | - |
dc.description.abstract | 到目前為止,已知至少二十種人類蛋白質能夠產生纖維狀結構的類澱粉聚集,同時造成類澱粉症。類澱粉症是由於蛋白質結構的摺疊錯誤造成聚集的生成,此類聚集以纖維狀的結構彼此糾結,並且導致細胞與組織的病變。雖然知道類澱粉纖維會誘發疾病,但是對其病理機制至今仍無法完全了解。
本研究利用生物體內常見的穀胱甘肽(glutathione, GSH)當作還原劑,透過不同濃度GSH的添加來觀察雞蛋白溶菌酶(hen-egg-white lysozyme)和alpha-乳清蛋白(alpha-lactalbumin)兩種蛋白質產生類澱粉纖維行為之影響,並針對了GSH與蛋白質中雙硫鍵的反應來進行探討。本研究利用了多種分析方法,結果發現在55 oC與55 rpm之環境下可以成功地將溶菌酶與alpha-乳清蛋白誘導產生類澱粉纖維;添加5 mM GSH可以完全抑制alpha-乳清蛋白形成類澱粉纖維,而需10 mM GSH才能完全抑制溶菌酶形成類澱粉纖維;隨著GSH濃度的上升可以明顯地增加溶菌酶類澱粉纖維成長之延遲期,但是對於alpha-乳清蛋白幾乎沒有影響。當alpha-乳清蛋白與溶菌酶放置於GSH環境中超過24小時後,電泳結果會出現裂解的現象。從DTNB-GdnHCl的實驗中發現,alpha-乳清蛋白中的雙硫鍵會隨著GSH的添加而造成斷裂,GSH濃度越高雙硫鍵斷裂數目越多,至於未添加GSH的alpha-乳清蛋白並沒有發現雙硫鍵的斷裂。然而,未添加GSH的溶菌酶就已經有雙硫鍵的斷裂,而添加不同濃度的GSH並不會使溶菌酶雙硫鍵斷裂數目增加,但卻會減緩雙硫鍵的斷裂速度。本研究之結果除了有助於解釋alpha-乳清蛋白與溶菌酶形成類澱粉纖維之機制,以及雙硫鍵的斷裂對於類澱粉纖維之影響外,並可更進一步地對類澱粉症之抑制提供有效的策略。 | zh_TW |
dc.description.abstract | At least twenty different human proteins can form species with fibrillar structure resulting in a variety of human diseases called amyloidosis. These proteins are capable of misfolding or self-assembling into stable fibrils with a characteristic cross-beta pleated sheet secondary structure. Although amyloid diseases have been the center of intense research, the role of amyloid protein and the toxicity mechanisms that mediate its biological responses remain largely unknown.
In this research, we examined the effects of reduced form of glutathione (GSH) on the in vitro fibrillogenesis of bovine alpha-lactalbumin and hen-egg-white lysozyme at acidic pH (pH 2.0) and also focused on the interaction(s) between GSH and the disulfide bonds of these two proteins. Using ThT fluorescence, Congo red binding, ANS-fluorescence, and circular dichroism spectroscopy, we found that the native structure of alpha-lactalbumin or lysozyme was successfully converted into amyloid fibrils at 55 oC and 55 rpm. The formation of fibrils was completely inhibited in the presence of 5 mM and 10 mM GSH for alpha-lactalbumin and lysozyme, respectively. The growth of lysozyme fibrils was significantly delayed by the increase in GSH concentration but this behavior was not observed in the case of alpha-lactalbumin. When alpha-lactalbumin or lysozyme incubated with GSH for more than 24 hours, the acid cleavage/fragmentation was observed on the SDS-PAGE gels. We showed in the results of sulfhydryl content determination the number of disrupted disulfide bonds of alpha-lactalbumin, starting from 0 in its native state, increased with increasing concentration of GSH. As for lysozyme, samples with or without GSH had broken disulfide bridges and the presence of GSH otherwise reduced the rate of disulfide bond disruption. We believe that the outcome from this work can not only help explain the mechanisms of the fibril formation for alpha-lactalbumin and lysozyme but also explore the roles of disulfide bond in amyloid fibrils. Furthermore, results from this study provide potential inhibitory strategies against the amyloid formation associated with amyloid diseases. | en |
dc.description.provenance | Made available in DSpace on 2021-06-13T15:33:57Z (GMT). No. of bitstreams: 1 ntu-97-R95524022-1.pdf: 3340976 bytes, checksum: 45c41d9651b4935aaaef3a465071ced2 (MD5) Previous issue date: 2008 | en |
dc.description.tableofcontents | 摘要 I
Abstract II 目錄 IIV 圖目錄 IX 表目錄 XII 第一章 緒論 1 第二章 文獻回顧 3 2-1 類澱粉症 (amyloidosis) 3 2-2 蛋白質結構 5 2-2-1 一級結構 7 2-2-2 二級結構 7 2-2-3 三級結構 8 2-2-4 四級結構 9 2-3蛋白質的摺疊(folding) 10 2-3-1 蛋白質的摺疊原理 10 2-3-2 蛋白質的摺疊構形 12 2-3-3 蛋白質結構間的作用力 12 2-3-3-1胜肽鍵 13 2-3-3-2 氫鍵 13 2-3-3-3 雙硫鍵 13 2-3-3-4 疏水性作用力 14 2-3-3-5 離子作用力 14 2-4 蛋白質的聚集 16 2-4-1 試管內的蛋白質聚集 16 2-4-1-1蛋白質結構的影響 17 2-4-1-2 外在環境的影響[24] 18 2-4-2 蛋白質聚集體的構造 19 2-5 溶菌酶(Lysozyme)之介紹 21 2-6 alpha-乳清蛋白(alpha-lactalbumin)之介紹 23 2-7蛋白質中的雙硫鍵 26 2-7-1 蛋白質中雙硫鍵的生成 27 2-7-2蛋白質中雙硫鍵的斷裂 27 2-7-2-1金屬離子 27 2-7-2-2 亞硫酸鹽(sulfite)與氰化物(cyanide) 28 2-7-2-3 單硫磷酸(monothiophosphoric acid)與三級三氫化磷(tertiary phosphines) 29 2-7-2-4 Sodium borohydride (NaBH4) 30 2-7-2-5 鹼性環境(alkaline medium) 30 2-7-2-6硫醇基 31 2-7-3 雙硫鍵間之置換反應(disulfide exchange) 34 2-7-4 硫醇基-雙硫鍵置換反應 35 2-7-5 雙硫鍵與膠化現象(gelation) 36 2-8 氧化還原緩衝液(redox buffer) 39 2-8-1 穀胱甘肽 41 2-9 研究蛋白質聚集常見之偵測方法 45 2-9-1 ThT螢光放射 45 2-9-2 剛果紅鍵結 45 2-9-3 ANS螢光測試 46 2-9-4 圓二色光譜分析 47 2-9-5 蛋白質中硫醇基之測量 49 2-9-5-1 總硫醇基、曝露(exposed)之硫醇基與埋藏(buried)之硫醇基 51 2-9-6 蛋白質濃度測定 52 2-9-7 膠體電泳(gel electrophoresis) 52 第三章 研究動機 54 第四章 實驗裝置、藥品與步驟 55 4-1 實驗儀器 55 4-2 實驗藥品 56 4-3 實驗步驟 58 4-3-1 蛋白質樣品製備 58 4-3-2 ThT螢光光譜分析(Thioflavin T fluorescence spectroscopy) 58 4-3-3 剛果紅染劑鍵結分析(Congo red biding assay) 58 4-3-4 ANS螢光光譜分析(ANS fluorescence spectrometry) 59 4-3-5 遠紫外光圓二色光譜分析(Far-UV CD spectroscopy) 59 4-3-6 DTNB染劑鍵結分析(DTNB binding assay) 60 4-3-7 DTDP染劑鍵結分析(DTDP binding assay) 60 4-3-8 胍鹽酸實驗方法 60 4-3-9 透析實驗方法 60 4-3-10 BCA蛋白質濃度分析(BCA assay) 61 4-3-11 穿透式電子顯微鏡(Transmission electron microscopy, TEM) 61 4-3-12 蛋白質電泳(Protein gel electorphoresis) 62 4-3-12-1 製做SDS-PAGE膠片 62 4-3-12-2 蛋白質電泳實驗 62 第五章 實驗結果與討論 64 5-1 不同濃度之GSH對alpha-乳清蛋白形成類澱粉纖維之影響 64 5-1-1 利用酸性環境誘導alpha-乳清蛋白類澱粉纖維之形成 64 5-1-2 不同濃度GSH對於alpha-乳清蛋白形成類澱粉纖維之影響 67 5-1-3 疏水性區域的裸露對於alpha-乳清蛋白類澱粉纖維形成之探討 72 5-1-4 不同濃度的GSH對alpha-乳清蛋白之二級結構的影響 74 5-2 不同濃度的GSH對雞蛋白溶菌酶生成類澱粉纖維之影響 79 5-2-1 誘導雞蛋白溶菌酶生成類澱粉纖維 79 5-2-2 添加不同濃度GSH對於類澱粉纖維之影響 79 5-2-3 GSH濃度對於雞蛋白溶菌酶疏水性結構之變化 85 5-2-4 GSH濃度對於雞蛋白溶菌酶二級結構之變化 87 5-3 穿透式電子顯微鏡觀察類澱粉纖維之結果(TEM) 91 5-4-1 alpha-乳清蛋白之電泳分析結果 95 5-4-2 溶菌酶之電泳分析結果 99 5-4-3 酸性環境對於蛋白質結構之影響 103 5-5 alpha-乳清蛋白與溶菌酶形成類澱粉纖維機制之比較與初步探討 106 5-6 GSH對於alpha-乳清蛋白與溶菌酶中雙硫鍵的影響 107 5-6-1 GSH對alpha-乳清蛋白中雙硫鍵之影響 109 5-6-2 GSH對溶菌酶中雙硫鍵之影響 111 5-6-3 酸性環境以及GSH對雙硫鍵斷裂之影響 114 5-7 實驗結果整理與比較 116 第六章 結論與建議 120 6-1類澱粉纖維形成之機制與GSH之影響 120 6-1-1 alpha-乳清蛋白以及溶菌酶誘導形成類澱粉纖維之機制 122 6-1-2 低濃度GSH抑制alpha-乳清蛋白以及溶菌酶誘導形成類澱粉纖維之機制 122 6-1-3 高濃度GSH抑制alpha-乳清蛋白以及溶菌酶誘導形成類澱粉纖維之機制 122 6-2 酸性環性與GSH對於蛋白質中雙硫鍵的影響與結果 124 6-2-1 alpha-乳清蛋白的雙硫鍵在酸性與GSH環境下之變化 124 6-2-2 溶菌酶的雙硫鍵在酸性與GSH環境下之變化 125 6-3 建議 127 參考文獻 128 附錄 144 附錄A濃度校正曲線 144 附錄B alpha-乳清蛋白與溶菌酶類澱粉纖維成長動力學 147 | |
dc.language.iso | zh-TW | |
dc.title | 探討還原劑對於乳清蛋白類澱粉纖維形成之影響 | zh_TW |
dc.title | Examining the Effect of Reducing Agent on the Amyloid
Fibril Formation of Alpha-Lactalbumin | en |
dc.type | Thesis | |
dc.date.schoolyear | 96-2 | |
dc.description.degree | 碩士 | |
dc.contributor.oralexamcommittee | 劉懷勝(Hwai-Shen Liu),胡朝榮,王昱麒,侯劭毅 | |
dc.subject.keyword | 類澱粉纖維,乳清蛋白,溶菌酶,穀胱甘肽,還原劑,雙硫鍵, | zh_TW |
dc.subject.keyword | amyloid,fibril,alpha-lactalbumin,lysozyme,glutathione,reducing agent,disulfide bond, | en |
dc.relation.page | 148 | |
dc.rights.note | 有償授權 | |
dc.date.accepted | 2008-07-14 | |
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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