Breydo Leonid, Makarava Natallia, Baskakov Ilia V
Medical Biotechnology Center, University of Maryland Biotechnology Institute, Baltimore, MD, USA.
Methods Mol Biol. 2008;459:105-15. doi: 10.1007/978-1-59745-234-2_8.
Misfolding and aggregation of prion protein (PrP) is related to several neurodegenerative diseases in humans such as Creutzfeldt-Jacob disease, fatal familial insomnia, and Gerstmann-Straussler-Sheinker disease. Amyloid fibrils prepared from recombinant PrP in vitro share many features of the infectious prions. These fibrils can be used as a synthetic surrogate of PrP(Sc) for development of prion diagnostics, including generation of PrP(Sc)-specific antibody, for screening of antiprion drugs, or for development of antiprion decontamination procedures. Here, we describe the methods of preparation of prion protein fibrils in vitro and biochemical assays for assessing physical properties and the quality of fibrils.
朊病毒蛋白（PrP）的错误折叠和聚集与人类的几种神经退行性疾病有关，如克雅氏病、致死性家族性失眠症和格斯特曼-施特劳斯勒-谢克尔病。体外由重组PrP制备的淀粉样纤维具有传染性朊病毒的许多特征。这些纤维可用作PrP(Sc)的合成替代物，用于朊病毒诊断的开发，包括生成PrP(Sc)特异性抗体、筛选抗朊病毒药物或开发抗朊病毒去污程序。在此，我们描述了体外制备朊病毒蛋白纤维的方法以及用于评估纤维物理性质和质量的生化分析方法。
