Prion pathologies are fatal neurodegenerative diseases caused by the misfolding of the physiological Prion Protein (PrP^C) into a β-structure-rich isoform called PrP^Sc. To date, there is no available cure for prion diseases and just a few clinical trials have been carried out. The initial approach in the search of anti-prion agents had PrP^Sc as a target, but the existence of different prion strains arising from alternative conformations of PrP^Sc, limited the efficacy of the ligands to a straindependent ability. That has shifted research to PrP^C ligands, which either act as chaperones, by stabilizing the native conformation, or inhibit its interaction with PrP^Sc. The role of transition-metal mediated oxidation processes in prion misfolding has also been investigated. Another promising approach is the indirect action via other cellular targets, like membrane domains or the Protein- Folding Activity of Ribosomes (PFAR). Also, new prion-specific high throughput screening techniques have been developed. However, so far no substance has been found to be able to extend satisfactorily survival time in animal models of prion diseases. This review describes the main features of the Structure-Activity Relationship (SAR) of the various chemical classes of anti-prion agents.

on病毒病理学是致命的神经退行性疾病，由生理性Pri病毒蛋白质（PrP ^C）错折叠为富含β结构的同工型PrP ^Sc引起。迄今为止，尚无可治愈病毒疾病的方法，仅进行了一些临床试验。寻找抗-病毒剂的最初方法是以PrP ^Sc为靶标，但是由于PrP ^Sc的替代构象而产生的不同病毒菌株的存在，使配体的功效受限于菌株依赖性能力。这就将研究转移到了PrP ^C配体上，它们通过稳定天然构象或抑制其与PrP ^Sc的相互作用而充当分子伴侣。。还研究了过渡金属介导的氧化过程在病毒错折叠中的作用。另一种有希望的方法是通过其他细胞靶标的间接作用，例如膜结构域或核糖体的蛋白折叠活性（PFAR）。而且，已经开发了新的病毒特异性的高通量筛选技术。但是，到目前为止，在病毒疾病的动物模型中，没有发现能够延长令人满意的生存时间的物质。这篇综述描述了抗chemical病毒剂的各种化学类别的结构-活性关系（SAR）的主要特征。