Untangling the interaction of α-synuclein with DNA i-motifs and hairpins by volume-sensitive single-molecule FRET spectroscopy.

Sanjib K MukherjeeJim-Marcel KnopRosario OlivaSimone MöbitzRoland Hermann Alfons Winter

Published in: RSC chemical biology (2021)

The intrinsically disordered protein α-synuclein causes Parkinson's disease by forming toxic oligomeric aggregates inside neurons. Single-molecule FRET experiments revealed conformational changes of noncanonical DNA structures, such as i-motifs and hairpins, in the presence of α-synuclein. Volumetric analyses revealed differences in binding mode, which is also affected by cellular osmolytes.

Keyphrases

single molecule
living cells
atomic force microscopy
single cell
spinal cord
binding protein
high resolution
mass spectrometry
spinal cord injury
transcription factor