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-electron tomography. We estimated the number of monomeric protein units present in these minute structures. This approach is ideally suited for the investigation of the molecular mechanisms of amyloid formation both in vitro and in the cellular milieu.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
Roberti MJ,Fölling J,Celej MS,Bossi M,Jovin TM,Jares-Erijman EAdoi
10.1016/j.bpj.2012.03.010subject
Has Abstractpub_date
2012-04-04 00:00:00pages
1598-607issue
7eissn
0006-3495issn
1542-0086pii
S0006-3495(12)00292-5journal_volume
102pub_type
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