Characterizing Prion-Like Protein Aggregation: Emerging Nanopore-Based Approaches

Prion-like protein aggregation is characteristic of numerous neurodegenerative diseases, such as Alzheimer's and Parkinson's diseases. This process involves the formation of aggregates ranging from small and potentially neurotoxic oligomers to highly structured self-propagating amyloid fibrils. Various approaches are used to study protein aggregation, but they do not always provide continuous information on the polymorphic, transient, and heterogeneous species formed. This review provides an updated state-of-the-art approach to the detection and characterization of a wide range of protein aggregates using nanopore technology. For each type of nanopore, biological, solid-state polymer, and nanopipette, discuss the main achievements for the detection of protein aggregates as well as the significant contributions to the understanding of protein aggregation and diagnostics. Prion-like protein aggregation, a hallmark of several neurodegenerative diseases like Alzheimer's and Parkinson's, involves the formation of oligomers and amyloid fibrils. This review outlines the use of nanopore technology including biological, solid-state, polymer, and nanopores as well as nanopipette, for detecting and characterizing protein aggregates. Their achievement for protein aggregation understanding and the application in diagnostics are discussed. image