C-Terminal Truncated α-Synuclein Fibrils Contain Strongly Twisted β-Sheets.

ABSTRACT: C-terminal truncations of monomeric wild-type alpha-synuclein (henceforth WT-αS) have been shown to enhance the formation of amyloid aggregates both in vivo and in vitro and have been associated with accelerated progression of Parkinson's disease (PD). The correlation with PD may not solely be a result of faster aggregation, but also of which fibril polymorphs are preferentially formed when the C-terminal residues are deleted. Considering that different polymorphs are known to result in distinct pathologies, it is important to understand how these truncations affect the organization of αS into fibrils. Here we present high-resolution microscopy and advanced vibrational spectroscopy studies that indicate that the C-terminal truncation variant of αS, lacking residues 109-140 (henceforth refe

SUBMITTER: Iyer A 

PROVIDER: S-EPMC5668890 | biostudies-literature | 2017 Nov

REPOSITORIES: biostudies-literature