Imaging nanometer-sized α-synuclein aggregates by superresolution fluorescence localization microscopy.

ABSTRACT: The morphological features of α-synuclein (AS) amyloid aggregation in vitro and in cells were elucidated at the nanoscale by far-field subdiffraction fluorescence localization microscopy. Labeling AS with rhodamine spiroamide probes allowed us to image AS fibrillar structures by fluorescence stochastic nanoscopy with an enhanced resolution at least 10-fold higher than that achieved with conventional, diffraction-limited techniques. The implementation of dual-color detection, combined with atomic force microscopy, revealed the propagation of individual fibrils in vitro. In cells, labeled protein appeared as amyloid aggregates of spheroidal morphology and subdiffraction sizes compatible with in vitro supramolecular intermediates perceived independently by atomic force microscopy and cryo-ele

SUBMITTER: Roberti MJ 

PROVIDER: S-EPMC3318128 | biostudies-literature | 2012 Apr

REPOSITORIES: biostudies-literature