Amyloid fibrils and fibril-like structures are currently estimated to represent many different products of several genes in humans and play a key role in many types of proteinopathies, commonly associated with ageing process. They share the mutual feature of aggregation-prone proteins and the building up of molecular-supramolecular structure, such as inter-neuronal plaques in the brain of Alzheimer’s Disease (AD) patients, characterized by an extraordinary strength. Noteworthy, this type of structure has been reported in different organisms, in particular in invertebrates. The aim of the current review is to focus on alpha and beta amyloids i.e., SAAs, SAP and APP, elucidating the structure and function of amyloid proteins in invertebrates (such as nematods, annelids, molluscs, insects, ascidians) and highlighting their striking pattern of functional conservation when compared to human amyloid-like fibrils, thus focusing on possible new studies and applications for innovative therapies, particularly for AD, the most common and worldwide type of dementia.

目前估计淀粉样蛋白原纤维和原纤维样结构代表人类多种基因的许多不同产物，并且在通常与衰老过程相关的许多类型的蛋白质病中起关键作用。它们具有易于聚集的蛋白质和建立分子超分子结构的共同特征，例如阿尔茨海默病 (AD) 患者大脑中的神经元间斑块，其特点是具有非凡的强度。值得注意的是，这种类型的结构已在不同的生物体中得到报道，特别是在无脊椎动物中。本综述的目的是关注 α 和 β 淀粉样蛋白，即 SAA、SAP 和 APP，阐明淀粉样蛋白在无脊椎动物（如线虫、环节动物、软体动物、昆虫、