Exploring the Impact of Physiological C-Terminal Truncation on α-Synuclein Conformations to Unveil Mechanisms Regulating Pathological Aggregation.

ABSTRACT: Emerging evidence suggests that physiological C-terminal truncation of α-synuclein (αS) plays a critical role in regulating liquid-liquid phase separation and promoting amyloid aggregation, processes implicated in neurodegenerative diseases such as Parkinson's disease (PD). However, the molecular mechanisms through which C-terminal truncation influences αS conformation and modulates its aggregation remain poorly understood. In this study, we investigated the impact of C-terminal truncation on αS conformational dynamics by comparing full-length αS_1-140 with truncated αS_1-103 monomers using atomistic discrete molecular dynamics simulations. Our findings revealed that both αS_1-140 and αS_1-103 primarily adopted helical conformations around residues 7

SUBMITTER: Huang F 

PROVIDER: S-EPMC11588551 | biostudies-literature | 2024 Nov

REPOSITORIES: biostudies-literature