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. 2021 Feb 23;60(9):678–688. doi: 10.1021/acs.biochem.1c00003

Figure 3.

Figure 3

Aβ42 fibrillation kinetics in the presence of proSP-C BRICHOS T187R. (A) Individual fits (colored lines) of normalized aggregation traces of 3 μM Aβ42 alone (black) and in the presence of 0.1, 0.3, 0.5, 1, and 1.5 molar equivalents of proSP-C BRICHOS T187R (light blue to dark blue empty circles) using a kinetic nucleation model in which the combined rate constants Inline graphic and Inline graphic are free fitting parameters. (B) Seeded reaction profiles of 3 μM Aβ42 with 0.6 μM preformed fibrils (black) in the presence of 0.1, 0.3, 0.5, 0.7, and 1.0 molar equivalent of proSP-C BRICHOS T187R (light pink to dark purple). Data represent the average of four replicates. The black rectangle shows a close-up of the onset of aggregation. Colored lines are corresponding fits to the data using a linear regression. (C) Effects of relative rate constants knk+ (green), k+ (pink), and k+k2 (blue) from the fits shown in panels A and B. Rates have been normalized to Aβ42 in the absence of BRICHOS. Data represent the mean ± the standard deviation of four or five replicates.