Abstract

Although first described in the context of disease, cross-β (amyloid) fibrils have also been found as functional entities in all kingdoms of life. However, what are the specific properties of the cross-β fibril motif that convey biological function, make them especially suited for their particular purpose, and distinguish them from other fibrils found in biology? This review approaches these questions by arguing that cross-β fibrils are highly periodic, stable, and self-templating structures whose formation is accompanied by substantial conformational change that leads to a multimerization of their core and framing sequences. A discussion of each of these properties is followed by selected examples of functional cross-β fibrils that show how function is usually achieved by leveraging many of these properties.

摘要

尽管最初是在疾病背景下描述的，但交叉 β（淀粉样蛋白）原纤维也被发现是所有生命领域的功能实体。然而，跨β原纤维基序有哪些具体特性可以传递生物学功能，使它们特别适合其特定目的，并将它们与生物学中发现的其他原纤维区分开来？本综述通过认为交叉β原纤维是高度周期性、稳定和自模板结构，其形成伴随着显着的构象变化，从而导致其核心和框架序列的多聚化，从而解决了这些问题。对这些特性的讨论之后是功能性交叉β原纤维的选定示例，这些示例展示了通常如何通过利用许多这些特性来实现功能。