Pre-aggregation kinetics and intermediates of α-synuclein monitored by the ESIPT probe 7MFE.

ABSTRACT: The defining feature of the extensive family of amyloid diseases is the formation of networks of entangled elongated protein fibrils and amorphous aggregates exhibiting crossed β-sheet secondary structure. The time course of amyloid conversion has been studied extensively in vitro with the proteins involved in the neurodegenerative pathology of Parkinson's disease (α-synuclein), Alzheimer's disease (Tau) and Huntington's disease (Huntingtin). Although much is known about the thermodynamics and kinetics of the transition from a soluble, intrinsically disordered monomer to the fibrillar end state, the putative oligomeric intermediates, currently considered to be the major initiators of cellular toxicity, are as yet poorly defined. We have detected and characterized amyloid precursors by moni

SUBMITTER: Fauerbach JA 

PROVIDER: S-EPMC5982440 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature