Journal: Molecules

Article Title: The Amyloid Fibril-Forming β-Sheet Regions of Amyloid β and α-Synuclein Preferentially Interact with the Molecular Chaperone 14-3-3ζ

doi: 10.3390/molecules26206120

Figure Lengend Snippet: The molecular chaperone ability of 14-3-3ζ to inhibit amyloid fibril formation of Aβ 40 and Aβ 42 . Amyloid fibril formation, as monitored by ThT fluorescence, of 15 μM Aβ 40 ( A ) and Aβ 42 ( B ) at 37 °C in the absence (black circles) and presence of 14-3-3ζ at 1.0:0.5 (brown triangles; Aβ 40 only), 1:1 (red crosses), and 1:2 (blue diamonds) molar ratios of Aβ 40 /Aβ 42 :14-3-3ζ. Also shown is 14-3-3ζ incubated alone at 30 µM (beige squares). On the right of part ( A ) are TEM images of Aβ 40 in the absence and presence of 14-3-3ζ at a 1.0:0.5 molar ratio of Aβ 40 :14-3-3ζ. Samples for TEM imaging were taken upon completion of the aggregation assay after 150 h of incubation. On the right of part ( B ) are TEM images of Aβ 42 in the absence and presence of 14-3-3ζ at an equimolar ratio. Each image was acquired from the samples after 200 min. of incubation. Scale bars in all images represent 1 μm.

Article Snippet: An aliquot of the protein solutions from in situ ThT assays (6 μL) was transferred onto a carbon-coated nickel transmission electron microscopy (TEM) grid (SPI Supplies, West Chester, PA, USA).

Techniques: Fluorescence, Incubation, Imaging