Detection of Transient Interchain Interactions in the Intrinsically Disordered Protein α-Synuclein by NMR Paramagnetic Relaxation Enhancement

摘要

Protein aggregation and amyloid fibril formation are associated with a wide range of neurodegenerative diseases, including Alzheimer's, Parkinson's, and Prion disease. Despite numerous studies on protein aggregation, the mechanism by which proteins are converted from their normally soluble form to insoluble amyloid fibrils is still not well understood. Amyloid fibril formation for α-synuclein (αSyn), the primary protein component in Parkinson's disease, begins from an ensemble of heterogeneous intrinsically disordered conformations.