Single point mutations at the S129 residue of α-synuclein and their effect on structure, aggregation, and neurotoxicity.

ABSTRACT: Parkinson's disease is an age-related neurological disorder, and the pathology of the disease is linked to different types of aggregates of α-synuclein or alpha-synuclein (aS), which is an intrinsically disordered protein. The C-terminal domain (residues 96-140) of the protein is highly fluctuating and possesses random/disordered coil conformation. Thus, the region plays a significant role in the protein's solubility and stability by an interaction with other parts of the protein. In the current investigation, we examined the structure and aggregation behavior of two artificial single point mutations at a C-terminal residue at position 129 that represent a serine residue in the wild-type human aS (wt aS). Circular Dichroism (CD) and Raman spectroscopy were performed to analyse the secondar

SUBMITTER: Pandit E 

PROVIDER: S-EPMC10250651 | biostudies-literature | 2023

REPOSITORIES: biostudies-literature