Protein misfolding and aggregation into highly ordered fibrillar structures have been traditionally associated with pathological processes. Nevertheless, nature has taken advantage of the particular properties of amyloids for functional purposes, like in the protection of organisms against environmental changing conditions. Over the last decades, these fibrillar structures have inspired the design of new nanomaterials with intriguing applications in biomedicine and nanotechnology such as tissue engineering, drug delivery, adhesive materials, biodegradable nanocomposites, nanowires or biosensors. Prion and prion-like proteins, which are considered a subclass of amyloids, are becoming ideal candidates for the design of new and tunable nanomaterials. In this review, we discuss the particular properties of this kind of proteins, and the current advances on the design of new materials based on prion sequences.

蛋白质错误折叠和聚集成高度有序的纤维结构传统上与病理过程相关。然而，大自然已经利用淀粉样蛋白的特殊性质来实现功能目的，例如保护生物体免受环境变化条件的影响。在过去的几十年里，这些纤维结构激发了新型纳米材料的设计，在生物医学和纳米技术中具有有趣的应用，例如组织工程、药物输送、粘合材料、可生物降解的纳米复合材料、纳米线或生物传感器。朊病毒和类朊病毒蛋白被认为是淀粉样蛋白的一个亚类，正在成为设计新型可调节纳米材料的理想候选者。在这篇综述中，我们讨论了此类蛋白质的特殊性质，以及基于朊病毒序列的新材料设计的最新进展。