Protein amyloid aggregate: Structure and function

Abstract

Abstract Protein amyloid aggregation has been widely observed to occur and plays important roles in both physiological processes and pathological diseases. Remarkably, amyloid aggregates assembled by native proteins gain a variety of different biological activities, which cannot be adopted by the unassembled protein alone. Thus, it is important to investigate the molecular basis of self‐assembly of protein amyloid aggregates and how the aggregated protein structure determines its function. In the review, we firstly introduce our structural knowledge on how different amyloid proteins undergo conformational transition and assemble into amyloid aggregate, with the main focus on amyloid fibril, which is the major species of amyloid aggregate. Then, we elaborate how different structures of amyloid fibrils enable them to fulfill highly diverse functions in either physiological or pathological condition. Furthermore, we discuss the structural polymorph which is a very unique feature of amyloid fibril, and its implication in understanding the structure‐function relationship of amyloid fibrils. Finally, we point out the importance of applying and integrating new approaches for deepening the structure‐function study of amyloid fibrils and highlight the potential of designing amyloid fibril‐based functional bio‐nanomaterials for application.

Keywords

• amyloid fibril
• neurodegenerative diseases
• prion‐like propagation
• protein phase separation
• protein aggregate