Fig. 5: Quantification of Aβ40 oligomer sizes by time-resolved light scattering. | Nature Communications

Fig. 5: Quantification of Aβ40 oligomer sizes by time-resolved light scattering.

From: Early events in amyloid-β self-assembly probed by time-resolved solid state NMR and light scattering

Fig. 5

a Light scattering signals, measured as photomultiplier tube voltages, for a 1.5 mM Aβ40 solution at pH 12 (cyan), a 1.5 mM Aβ40 solution after a rapid pH drop from 12 to 7.4 (red), and a pH 7.4 buffer alone (blue). Dashed line is a stretched-exponential fit to the pH drop data, as described in the text. Inset shows the data up to 50 ms. b Light scattering data recorded to 3600 s after a rapid pH drop. Insets compare the data up to 3.0 s (red) with pH drop data from a (orange). Dashed line is an empirical fit to a function that includes two stretched-exponential terms to describe curvature on 100 ms and 100 s time scales and a linear term to describe the long-time behavior, as described in the text. c Fits of the experimental data (dashed line) with simulations based on the coagulation model described in the text. Simulations parameters r0 and E0 were optimized for each value of the threshold size Nth, below which oligomer fusion rates r0 are multiplied by the enhancement factor of E0. Experimental and simulated light scattering signals are normalized to the signal from a 1.0 mM solution of monomeric Aβ40. d Dependences of the optimized values of r0 and E0 and the deviation between optimized simulations and experimental data on the assumed oligomer threshold size Nth. The best fit is obtained with Nth ≈ 16. Source data are provided as a Source data file.

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