Folding of N-terminally acetylated α-synuclein upon interaction with lipid membranes.

ABSTRACT: α-Synuclein (α-syn) is an abundant presynaptic neuronal protein whose aggregation is strongly associated with Parkinson's disease. It has been proposed that lipid membranes significantly affect α-syn's aggregation process. Extensive studies have been conducted to understand the interactions between α-syn and lipid membranes and have demonstrated that the N-terminus plays a critical role. However, the dynamics of the interactions and the conformational transitions of the N-terminus of α-syn at the atomistic scale details are still highly desired. In this study, we performed extensive enhanced sampling molecular dynamics simulations to quantify the folding and interactions of wild-type and N-terminally acetylated α-syn when interacting with lipid structures. We found that N-terminal acetylat

SUBMITTER: Tang Z 

PROVIDER: S-EPMC11560312 | biostudies-literature | 2024 Nov

REPOSITORIES: biostudies-literature