期刊
BIOPHYSICAL JOURNAL
卷 102, 期 7, 页码 1598-1607出版社
CELL PRESS
DOI: 10.1016/j.bpj.2012.03.010
关键词
-
类别
资金
- Max Planck Society
- Agencia Nacional de Promocion Cientifica y Tecnologica
- Consejo Nacional de Investigaciones Cientificas y Tecnicas (CONICET)
- Universidad de Buenos Aires Cientifica y Tecnologica
- Deutsche Forschungsgemeinschaft Centre for Molecular Physiology of the Brain (DFG CMPB)
- CMPB, in Gottingen
The morphological features of a-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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据