Structure, assembly, and biological activity of amyloid peptides and proteins.

淀粉样原纤维是由多种不同的蛋白质和肽形成的高度有序的丝状结构。 这些组装体最初被描述为淀粉样变性中细胞毒性的潜在介质，并且与朊病毒疾病的感染性有关。 最近，淀粉样蛋白被证明在多种生物过程中发挥着重要的功能作用，包括皮肤黑色素的组装、真菌和酵母的遗传多样性以及生物膜形成过程中细菌和酵母对表面的粘附。 尽管它们具有重要的生物学意义，但人们对多种蛋白质自组装成具有高度不同功能的密切相关结构的能力仍然知之甚少。 同样，目前尚不清楚这些组件中的一些组件如何具有有效的细胞毒性，而另一些组件则如何避免毒性以执行生物学任务。 这种建立在有序支架上的化学和功能多样性也是新型生物材料开发中的一个理想特征。 了解淀粉样蛋白在生物学中的作用，并开发其材料潜力，都需要详细了解原纤维形成的分子基础，以及将序列与原纤维状态的结构和功能联系起来的能力。

Amyloid fibrils are highly ordered filamentous structures formed by a wide range of different proteins and peptides. These assemblies were originally described as potential mediators of cytotoxicity in amyloidosis, and are linked to infectivity in prion diseases. More recently, amyloids been shown to play important functional roles in diverse biological processes ranging from assembly of the skin pigment melanin, genetic diversification of fungi and yeast and adhesion of bacteria and yeast to surfaces during biofilm formation. Despite their biological importance, the ability of diverse proteins to self-assemble into closely related structures having highly divergent function remains poorly understood. Similarly, it is not known how some of these assemblies can be potently cytotoxic while others avoid toxicity to perform biological tasks. This chemical and functional diversity, built on an ordered scaffold, is also a desirable feature in the development of novel biomaterials. Understanding the roles of amyloid proteins in biology, and exploiting their materials potential, both require detailed knowledge of the molecular basis for fibril formation, and the ability to link sequence with the structure and function of the fibrillar state.