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Related Concept Videos

Super-resolution Fluorescence Microscopy01:37

Super-resolution Fluorescence Microscopy

Super-resolution fluorescence microscopy (SRFM) provides a better resolution than conventional fluorescence microscopy by reducing the point spread function (PSF). PSF is the light intensity distribution from a point that causes it to appear blurred. Due to PSF, each fluorescing point appears bigger than its actual size, and it is the PSF interference of nearby fluorophores that causes the blurred image. Various approaches to achieving higher resolution through SRFM have recently been developed.

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Related Experiment Video

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Super-Resolution Imaging to Study Co-Localization of Proteins and Synaptic Markers in Primary Neurons
14:02

Super-Resolution Imaging to Study Co-Localization of Proteins and Synaptic Markers in Primary Neurons

Published on: October 31, 2020

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

M Julia Roberti1, Jonas Fölling, M Soledad Celej

  • 1Departamento de Química Orgánica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Ciudad Universitaria, Buenos Aires, Argentina.

Biophysical Journal
|April 17, 2012
PubMed
Summary
This summary is machine-generated.

Researchers visualized alpha-synuclein (AS) amyloid aggregation using advanced microscopy, revealing nanoscale structures and propagation mechanisms in vitro and in cells. This offers new insights into amyloid formation. Keywords: alpha-synuclein, amyloid aggregation, nanoscale imaging, microscopy.

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Super-Resolution Imaging to Study Co-Localization of Proteins and Synaptic Markers in Primary Neurons
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Published on: October 31, 2020

Super-resolution Imaging of Neuronal Dense-core Vesicles
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Super-resolution Imaging of Neuronal Dense-core Vesicles

Published on: July 2, 2014

Area of Science:

  • Biophysics
  • Cell Biology
  • Neuroscience

Background:

  • Alpha-synuclein (AS) aggregation into amyloid fibrils is central to neurodegenerative diseases like Parkinson's.
  • Understanding the nanoscale morphology and dynamics of AS aggregation is crucial for elucidating disease mechanisms.

Purpose of the Study:

  • To elucidate the nanoscale morphological features of alpha-synuclein (AS) amyloid aggregation in vitro and in cells.
  • To investigate the propagation mechanisms of AS fibrils using advanced imaging techniques.

Main Methods:

  • Far-field subdiffraction fluorescence localization microscopy (FSM) with rhodamine spiroamide probes.
  • Fluorescence stochastic nanoscopy (FSN) for enhanced resolution (10x higher than conventional microscopy).
  • Dual-color detection combined with Atomic Force Microscopy (AFM) and Cryo-Electron Tomography (Cryo-ET).

Main Results:

  • AS fibrillar structures were imaged at nanoscale resolution, revealing morphology and propagation in vitro.
  • In cells, AS appeared as spheroidal amyloid aggregates of subdiffraction sizes.
  • These cellular aggregates were compatible with in vitro supramolecular intermediates, and the number of monomeric units was estimated.

Conclusions:

  • The study provides nanoscale insights into AS amyloid formation in both cell-free and cellular environments.
  • The advanced microscopy approach is well-suited for investigating the molecular mechanisms of amyloidogenesis.
  • This technique enables detailed characterization of amyloid intermediates and their dynamics.