ABSTRACT

Amyloids display a highly ordered fibrillar structure. Many of these assemblies appear associated with human disease. However, the controllable, stable, tunable, and robust nature of amyloid fibrils can be exploited to build up remarkable nanomaterials with a wide range of applications in biomedicine and biotechnology. Functional prions constitute a particular class of amyloids. These transmissible proteins exhibit a modular architecture, with a disordered prion domain responsible for the assembly and one or more globular domains that account for the activity. Importantly, the original globular protein can be replaced with any protein of interest, without compromising the fibrillation potential. These genetic fusions form fibrils in which the globular domain remains folded, rendering functional nanostructures. However, in some cases, steric hindrance restricts the activity of these fibrils. This limitation can be solved by dissecting prion domains into shorter sequences that keep their self-assembling properties while allowing better access to the active protein in the fibrillar state. In this review, we will discuss the properties of prion-like functional nanomaterials and the amazing applications of these biocompatible fibrillar arrangements.

摘要

淀粉样蛋白显示出高度有序的纤维结构。许多这些组装似乎与人类疾病有关。然而，淀粉样原纤维的可控、稳定、可调和稳健的性质可用于构建卓越的纳米材料，在生物医学和生物技术领域具有广泛的应用。功能性朊病毒构成一类特殊的淀粉样蛋白。这些可传播的蛋白质表现出模块化结构，具有负责组装的无序朊病毒结构域和负责活性的一个或多个球状结构域。重要的是，原始的球状蛋白可以用任何感兴趣的蛋白替换，而不会影响纤维颤动的潜力。这些基因融合形成原纤维，其中球状结构域保持折叠，从而形成功能性纳米结构。然而，在某些情况下，空间位阻限制了这些原纤维的活性。这种限制可以通过将朊病毒结构域分割成更短的序列来解决，这些序列保持其自组装特性，同时允许更好地接触纤维状态的活性蛋白。在这篇综述中，我们将讨论类朊病毒功能纳米材料的特性以及这些生物相容性纤维排列的惊人应用。