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完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.advisor | 王勝仕 | |
dc.contributor.author | Chia-Min Lai | en |
dc.contributor.author | 賴佳閔 | zh_TW |
dc.date.accessioned | 2021-06-16T23:11:16Z | - |
dc.date.available | 2017-08-07 | |
dc.date.copyright | 2012-08-07 | |
dc.date.issued | 2012 | |
dc.date.submitted | 2012-08-03 | |
dc.identifier.citation | 參考文獻
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D. (1996) Spontaneous reconfiguration of adsorbed lysozyme layers observed by total internal reflection fluorescence with a pH-sensitive fluorophore, Langmuir 12, 6104-6113. 146. Kubiak-Ossowska, K., and Mulheran, P. A. (2010) Mechanism of Hen Egg White Lysozyme Adsorption on a Charged Solid Surface, Langmuir 26, 15954-15965. 147. Daly, S. M., Przybycien, T. M., and Tilton, R. D. (2003) Coverage-dependent orientation of lysozyme adsorbed on silica, Langmuir 19, 3848-3857. 148. Onuma, K., and Inaka, K. (2008) Lysozyme dimer association: Similarities and differences compared with lysozyme monomer association, J Cryst Growth 310, 1174-1181. 149. 林麗娟. (1994) X光繞射原理及其應用, 工業材料86期, 100-109. 150. Patterson, A. L. (1939) The Scherrer formula for x-ray particle size determination, Phys Rev 56, 978-982. | |
dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/64974 | - |
dc.description.abstract | 奈米粒子雖因其優越的物化特性而被廣泛地應用於電子、化妝品、與生醫等領域,然而其使用是否會對人體造成危害,仍有待進一步之研究。本研究以奈米二氧化鈰與奈米氧化鋅為系統,利用紫外光-可見光分光光度計、螢光光譜儀、圓二色光譜儀、界面電位分析儀等儀器及分析方法探討上述奈米粒子於pH7.4,37℃下對母雞蛋白溶菌酶之結構與活性的影響。實驗結果顯示奈米二氧化鈰不論吸附量,Freundlich親和常數,吸附強度與結合位點數都比氧化鋅高。於蛋白質二、三級結構方面,溶菌酶吸附上奈米二氧化鈰會使α-helix比例明顯下降且β-sheet及unorder比例上升;且由自體螢光光譜,螢光淬滅實驗、與Nile Red分析可知,溶菌酶之疏水區域有裸露之現象。相較於溶菌酶吸附於氧化鋅則不改變其二級結構,其疏水區域也只有些微裸露。此外,吸附於二氧化鈰上之溶菌酶活性有下降趨勢;而氧化鋅則幾乎保持其活性。氧化鋅對溶菌酶之穩定性也可由化學誘導蛋白質開展分析得之。於蛋白質二聚體與單體間之比例可發現,添加奈米粒子皆有促進二聚體生成之現象。由上述實驗結果推測溶菌酶之結構與活性改變與其吸附型態有關;推論之所以有不同吸附型態之產生可能與溶菌酶表面濃度與粒子表面性質相關。吾人推測溶菌酶以活性區對面之正電區域與奈米粒子表面鍵結,而由於氧化鋅表面溶菌酶多而限制溶菌酶結構開展;但二氧化鈰表面溶菌酶濃度較小,且溶菌酶正電區附近之極性胺基酸可能與二氧化鈰表面以氫鍵鍵結,加上曲率較大故會對結構造成扭曲破壞,進而影響其活性。我們相信本論文之結果將有助於對奈米粒子與生物分子間交互作用之瞭解。 | zh_TW |
dc.description.abstract | Nanoparticles are widely used in the fields of electronics, cosmetics, and biomedical given their superior physicochemical properties. However, nanoparticles may have adverse influence on the functions of proteins or impose potential threat to our lifes upon entering the human body.Using hen egg-white lysozyme as a model protein, we made attempts to examine the effects of two kinds of nanoparticles, nano-cerium oxide and nano-zinc oxide, on the structure and activity of hen egg white lysozyme in the condition of pH 7.4 and 37℃ using UV/vis spectrophotometer, fluorescence spectroscopy, circular dichroism spectroscopy, zetasizer , Nile red assay, and glutaraldehyde cross-linking with SDS-PAGE. Our experimental results demonstrate that the adsorption capacity, Freundlich affinity constant, adsorption strength and number of binding sites of lysozyme adsorption on nano-cerium oxide are larger than those on nano-zinc oxide. Also, the conformation of lysozyme upon its adsorption onto cerium oxide experiences transition of α-helix to β-sheet and un-order secondary structures. Intrinsic fluorescence spectroscopy, fluorescence quenching, and Nile red analyses show that the hydrophobic regions of lysozyme are exposed to solvent. For the adsorption of lysozyme onto nano-zinc oxide, almost no change is detected in the secondary structure, and the hydrophobic regions are only slightly exposed. In addition, the enzyme activity of lysozyme decreased when adsorbing onto the nano-cerium oxide, whereas the adsorption onto zinc oxide had shown no influence on its enzyme activity. Chemically induced protein unfolding analysis also pointed out that lysozyme adsorbed onto the nano-zinc oxide was more stable than that onto the cerium oxide . Furthermore, glutaraldehyde cross-linking studies indicated that a higher percentage of dimeric species of lysozyme were produced as compared to the monomeric species when lysozyme is conjugated with either the nanto-cerium oxide or nano-zinc oxide. Our results suggest that the changes of lysozyme structure and activity are correlated with its adsorption patterns, which may be associated with the surface concentration of lysozyme on nanoparticles and the surface properties of nanoparticles. We speculate that lysozyme adsorbs to the surface of nanoparticles using its positively charged patch on the protein surface, which is located at the opposite side of its active site. Moreover, the concentration of lysozyme adsorption on the nano-zinc oxide is significantly high so that the unfolding of lysozyme molecules is less likely to occur, thus no marked loss in enzyme activity is observed. On the contrary, the concentration of lysozyme adsorption on the nano-cerium oxide is relatively lower and some polar amino acid near the lysozyme’s positively charged patch may interact with the surface of the nano-cerium oxide through hydrogen bonding. This strong interaction/adsorption would lead to the distortion and destruction of lysozyme structure, thereby reducing its emzyme activity. We believe the outcome form this thesis may contribute to a better understanding of the interactions between nanoparticles and biomolecules. | en |
dc.description.provenance | Made available in DSpace on 2021-06-16T23:11:16Z (GMT). No. of bitstreams: 1 ntu-101-R99524027-1.pdf: 11671824 bytes, checksum: a2b7fe2be04aded7a572301245efbce6 (MD5) Previous issue date: 2012 | en |
dc.description.tableofcontents | 目錄
摘要 I Abstract II 目錄 IV 圖目錄 VIII 表目錄 XII 第一章 緒論 1 第二章 文獻回顧 3 2-1 蛋白質簡介 3 2-2-1 胺基酸 3 2-2-2 蛋白質結構 7 2-2-3 穩定蛋白質結構之作用力 16 2-2 溶菌酶簡介 20 2-2-1 溶菌酶種類 20 2-2-2 溶菌酶的生理功能 21 2-2-3 母雞蛋白溶菌酶之結構 23 2-2-4 母雞蛋白溶菌酶之活性 25 2-3 二氧化鈰簡介 27 2-3-2二氧化鈰之光學與化學性質 28 2-4 氧化鋅簡介 30 2-5 奈米科技 31 2-6 奈米材料之生物毒性 35 2-7 奈米粒子及材料與蛋白質之交互作用 38 2-7-1蛋白質冠冕(corona)形成 38 2-7-2奈米粒子及材料對蛋白質結構的影響 39 2-7-3奈米粒子及材料對蛋白質活性與穩定性的影響 41 2-7-4奈米粒子及材料對蛋白質纖維化(fibrillation)之影響 41 2-8 蛋白質於奈米粒子及材料上之吸附行為 51 2-8-1吸附量偵測 51 2-8-2吸附等溫曲線 51 2-8-3協同度(degree of coorperativity) 53 2-9 實驗檢測原理介紹 54 2-9-1自身螢光光譜(intrinsic fluorescence spectroscopy) 54 2-9-2螢光淬滅(fluorescence quenching) 57 2-9-3 Nile Red螢光光譜 59 2-9-4圓二色(CD)光譜方法 61 2-9-5戊二醛交聯(glutaldahyde crosslinking)暨SDS-PAGE蛋白質電泳方法(protein electrophoresis) 64 2-9-6粒徑電位分析儀(zetasizer) 66 2-9-7化學試劑誘導蛋白質開展(chemically induced protein unfolding) 69 2-9-8溶菌酶活性分析 71 第三章 研究動機 72 第四章 實驗儀器、藥品與步驟 73 4-1實驗裝置 73 4-2實驗藥品 74 4-3實驗方法和步驟 76 4-3-1奈米粒子製備 76 4-3-2 主要溶液配製 77 4-3-3二氧化鈰及氧化鋅物性偵測 77 4-3-4二氧化鈰與氧化鋅對母雞蛋白溶菌酶吸附與結構之影響 79 第五章 實驗結果與討論 92 5-1 二氧化鈰與氧化鋅奈米粒子之性質鑑定 92 5-1-1 粒徑大小 92 5-1-2 二氧化鈰與氧化鋅表面型態 93 5-1-3 二氧化鈰與氧化鋅之X光粉末繞射儀(XRPD)分析結果 95 5-1-4零電位點(the point of zero charge,PZC) 97 5-2母雞蛋白溶菌酶於不同奈米粒子上之吸附行為 98 5-2-1吸附等溫曲線 98 5-2-2協同度(degree of coorperativity) 103 5-2-3母雞蛋白溶菌酶吸附於奈米粒子之結合位點數 105 5-4 奈米粒子對母雞蛋白溶菌酶二級結構影響 107 5-4-1圓二色光譜(CD spectroscopy) 107 5-5二氧化鈰與氧化鋅對母雞蛋白溶菌酶三級結構影響 110 5-5-1自身螢光光譜(intrinsic fluorescence spectroscopy) 110 5-5-2 Nile Red螢光光譜 112 5-5-3螢光淬滅(fluorescence quenching) 114 5-6 溶菌酶吸附於氧化鋅與二氧化鈰之穩定性分析 118 5-6-1化學試劑誘導蛋白質開展(chemically induced protein unfolding) 118 5-7 二氧化鈰與氧化鋅對母雞蛋白溶菌酶活性之影響 121 5-8母雞蛋白溶菌酶於奈米粒子上之吸附對形成二聚體(dimer)的影響 124 5-8-1戊二醛交聯(glutaldehyde crosslinking)暨SDS-PAGE蛋白質電泳方法(protein electrophoresis) 124 5-9 溶菌酶與奈米粒子複合體之聚集現象 127 5-9-1粒徑與界面電位之變化 127 第六章 結論 129 第七章 未來展望 132 參考文獻 133 附錄 144 附錄A 溶菌酶吸附上奈米粒子之平衡時間 144 附錄B 溶菌酶對二氧化鈰之吸附計量比 146 附錄C 以end-on和side-on溶菌酶堆疊形式計算單層吸附量 147 附錄D 奈米粒子對溶菌酶活性影響之分析 149 附錄E quenching 平衡時間 151 附錄F The Scherrer Equation 152 | |
dc.language.iso | zh-TW | |
dc.title | 奈米二氧化鈰及氧化鋅對溶菌酶結構及活性之影響 | zh_TW |
dc.title | Effects of Nano-Cerium Oxide and Zinc Oxide on the Structure and Activity of Lysozyme | en |
dc.type | Thesis | |
dc.date.schoolyear | 100-2 | |
dc.description.degree | 碩士 | |
dc.contributor.oralexamcommittee | 王孟菊,林錕松,林達顯,詹正雄 | |
dc.subject.keyword | 奈米粒子,二氧化鈰,氧化鋅,溶菌酶,結構,活性,鍵結方位, | zh_TW |
dc.subject.keyword | nanoparticle,cerium oxide,zinc oxide,Hen egg white lysozyme(HEWL),structure,activity,binding site, | en |
dc.relation.page | 153 | |
dc.rights.note | 有償授權 | |
dc.date.accepted | 2012-08-03 | |
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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