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中文摘要：
β-淀粉样肽（Aβ）的聚集是导致阿尔茨海默病（AD）的主要原因之一。Aβ聚集物可以吸附在细胞膜表面，导致细胞凋亡，但有关细胞膜表面与Aβ相互作用的靶点分子尚不清楚。朊蛋白是一种位于细胞膜表面的糖蛋白，最近的研究表明朊蛋白可能是Aβ的作用靶点。基于AD当前的研究进展以及申请者在神经退行性疾病研究方面的工作基础，我们推测细胞型朊蛋白可能具有神经保护作用，但朊蛋白切割之后残留在细胞膜表面的片段有可能是Aβ聚集体的作用靶点，是引发Aβ毒性的源头。因此，我们拟采用表面等离子体激元共振（SPR）和荧光光谱等表面和溶液技术研究Aβ与朊蛋白切割前后多肽片断之间的相互作用，通过SPR技术检测Aβ在朊肽修饰膜表面的聚集过程、建立用于检测朊蛋白切割反应的分析方法，为认识朊蛋白在AD中的角色提供理论依据，对揭示朊蛋白的正常生理功能和理解AD的致病机制具有重要的意义。
结论摘要：
英文主题词Alzheimer’s disease；β-Amyloid；β-secretase；prion；biomarkers
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