3 research outputs found

    Oligomers and fibrils formation differentiated by ThT fluorescence.

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    <p>ThT fluorescence intensity was monitored to follow fibrillogenesis of Aβ(1–40) and Aβ(1–40)E22G in the presence and in the absence of 2 mM Ca<sup>2+</sup>. Black bars, Aβ(1–40) in phosphate buffer (“–Ca<sup>2+</sup> condition”); light grey bars, Aβ(1–40) in 2 mM CaCl<sub>2</sub>; dark grey bars, Aβ(1–40)E22G in phosphate buffer; light blue bars, Aβ(1–40)E22G in CaCl<sub>2</sub>. Shown are averages of values obtained in four independent experiments; error bars indicating the standard error of the average.</p

    ATR-FTIR spectra of Aβ(1–40) and Aβ(1–40)E22G.

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    <p>FTIR spectra of Aβ(1–40) and Aβ(1–40)E22G were taken in the presence and in the absence of added Ca<sup>2+</sup>, showing the amide I region of the spectra (1600–1700 cm<sup>−1</sup>). Aliquots of 2 µl were taken from each sample at <i>t</i> = 0, 2, 6, 24, 48, 72, and 96 h (shown in blue, green, red, cyan, purple, mustard, and dark blue, respectively). The data shown here were collected in one continuous experiment and are representative of three independent trials.</p

    Morphological comparison of Aβ(1–40) and Aβ(1–40)E22G.

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    <p>Contact mode AFM images (5 µm × 5 µm, Z scale 15 nm) of Aβ(1–40) and Aβ(1–40)E22G peptides on mica, recorded either in phosphate buffer or in MOPS buffer with Ca<sup>2+</sup>. Samples of Aβ(1–40) and Aβ(1–40)E22G in the presence and absence of added Ca<sup>2+</sup> (marked as “+Ca<sup>2+</sup>” or “−Ca<sup>2+</sup>”, respectively) at <i>t</i> = 0, 6, or 72 h. Closer views (1 µm × 1 µm, Z scale 15 nm) of oligomers, protofibrils and fibrils are shown as insets in the panel of <i>t</i> = 72 h (C, F, I, L). Images A, D, G, J were taken at <i>t</i> = 0; images B, E, H, K were taken at <i>t</i> = 6 h. Peptide concentration was the same in all samples.</p
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