Time-resolved detection of SDS-induced conformational changes in α-synuclein by a micro-stopped-flow system.

ABSTRACT: An intrinsically disordered protein, α-synuclein (αSyn), binds to negatively charged phospholipid membranes and adopts an α-helical structure. This conformational change is also induced by interaction with sodium dodecyl sulfate (SDS), which is an anionic surfactant used in previous studies to mimic membrane binding. However, while the structure of the αSyn and SDS complex has been studied widely by various static measurements, the process of structural change from the denatured state to the folded state remains unclear. In this study, the interaction dynamics between αSyn and SDS micelles was investigated using time-resolved measurements with a micro-stopped-flow system, which has been recently developed. In particular, the time-resolved diffusion based on the transient grating technique

SUBMITTER: Takaramoto S 

PROVIDER: S-EPMC8693425 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature