Structural features of α-synuclein amyloid fibrils revealed by Raman spectroscopy

• Published in: The Journal of biological chemistry Vol. 293; no. 3; pp. 767 - 776
• Main Authors: Flynn, Jessica D., McGlinchey, Ryan P., Walker, Robert L., Lee, Jennifer C.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 19.01.2018; American Society for Biochemistry and Molecular Biology
• Subjects: alpha-Synuclein - chemistry; alpha-Synuclein - genetics; alpha-Synuclein - ultrastructure; amyloid; Amyloid - chemistry; Amyloid - genetics; Amyloid - ultrastructure; electron microscopy (EM); fibril; Hydrogen-Ion Concentration; Microscopy, Electron, Transmission; mutant; Mutation; Parkinson Disease - metabolism; Parkinson's disease; Protein Conformation - drug effects; Protein Structure and Folding; Sodium Chloride - pharmacology; Spectrum Analysis, Raman - methods; fibril; amyloid; Parkinson's disease; mutant; electron microscopy (EM)

Parkinson’s disease (PD) is associated with the formation of α-synuclein amyloid fibrils. Elucidating the role of these β-sheet-rich fibrils in disease progression is crucial; however, collecting detailed structural information on amyloids is inherently difficult because of their insoluble, non-crys...