Electron Microscopy of Amyloid-Beta Peptide Oligomerization

Peptide oligomerization was also monitored by electron microscopy, as previously described [38 (link), 66 (link), 71 (link)]. Five microliters of either monomeric or oligomeric preparations of the different Aβ peptides were placed onto carbon-coated 400 mesh Cu/Rh grids (Ted Pella, Inc., Redding, CA) and stained with 1% uranyl acetate in distilled water (Polysciences, Inc., Warrington, PA). The stained grids were examined in a Philips CM-12 transmission electron microscope and photographed with a Gatan (4 k × 2.7 k) digital camera at the Image Core Facility of the Skirball Institute of Biomedical Medicine, NYU School of Medicine, as described [66 (link), 71 (link), 72 (link)].

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Rostagno A., Cabrera E., Lashley T, & Ghiso J. (2022). N-terminally truncated Aβ4-x proteoforms and their relevance for Alzheimer’s pathophysiology. Translational Neurodegeneration, 11, 30.

Publication 2022

carbon-coated 400 mesh Cu/Rh grids uranyl acetate CM-12 transmission electron microscope Gatan (4 k × 2.7 k) digital camera

Camera Carbon Electron microscopy Peptides Transmission electron microscope Uranyl acetate

Corresponding Organization :

Other organizations : New York University, University College London, National Hospital for Neurology and Neurosurgery

Top 5 similar protocols

Variable analysis

independent variables

Monomeric Aβ peptides
Oligomeric Aβ peptides

dependent variables

Peptide oligomerization
Morphology of peptide oligomers

control variables

Carbon-coated 400 mesh Cu/Rh grids
1% uranyl acetate in distilled water
Philips CM-12 transmission electron microscope
Gatan (4 k × 2.7 k) digital camera

controls

Positive control: Monomeric Aβ peptides
Negative control: Not specified

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