https://scholars.lib.ntu.edu.tw/handle/123456789/64935
標題: | 檢視愛滋海默症蛋白質與細胞膜間之交互作用以了解愛滋海默症之神經毒性機制 | 作者: | 王勝仕 | 公開日期: | 3-十一月-2004 | 出版社: | 臺北市:國立臺灣大學化學工程學系暨研究所 | 摘要: | 本研究擬利用表面電漿共振光譜技術對A摯瑬敳獩 與細胞膜間之鍵結或交互作用進行 及時觀測。表面電漿共振光譜技術之故乃在利用其高靈敏度、快速、即時、不需 標記及破壞分析物等之優點。細胞膜與A摯瑬敳獩 間之鍵結動力學行為是藉由SPR 光譜來 決定的,而細胞膜與A摯瑬敳獩 二成份間之交互作用是在金上鍍有一層特殊化合物之SPR chip 上進行。在接有磷脂質細胞膜SPR chip 上流過特定濃度之A摯瑬敳獩 溶液,以SPR 裝置紀錄鍵結行為。在經過特定計算公式求出結合常數與解離常數後,二者值之 比可得出親和性參數。嘗試找出親和能力數值與神經毒性間之關聯性,尋求細胞 培養神經毒性資料與分子階層生物物理模式間之關聯性,以對A摯瑬敳獩 細胞膜間交互作 用之機制與A摯瑬敳獩 誘發之神經毒性作進一步之探討與了解。 β -amyloid peptide (Aβ), the principal protein component of senile plaques in Alzheimer's disease (AD), plays an important role in neurotoxicity responsible for AD. Peptide structure and aggregation state are important in toxicity. However, the exact structure of the toxic form of the peptide and the mechanism by which it interacts with a cell to cause toxicity are unknown. This research was set out to use surface plasmon resonance (SPR) spectroscopy for the direct, real time observation of Aβ-membrane interaction. Via analyzing kinetic and equilibrium data obtained from SPR measurement, along with results from conventional biophysical and spectroscopic techniques as well as cell culture-based biological activity experiments, we will then construct a model, on a mechanistic/molecular level, of the interactions of Aβ-cell interaction, and seek for the link between biological toxicity and molecular/biophysical mechanisms of Alzheimer’s disease. We believe the results from this proposed research should lead to better understanding of membrane-amyloid peptide interactions that result in biological activity and further facilitate the development of new strategies/compounds to prevent amyloid protein (especially Aβ )-induced neurotoxicity. |
URI: | http://ntur.lib.ntu.edu.tw//handle/246246/9398 | 其他識別: | 922218E002035 | Rights: | 國立臺灣大學化學工程學系暨研究所 |
顯示於: | 化學工程學系 |
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922218E002035.pdf | 164.73 kB | Adobe PDF | 檢視/開啟 |
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