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. 2020 Jun 18;10(6):924. doi: 10.3390/biom10060924

Figure 5.

Figure 5

Fitting of the Aβ(1-42) aggregation kinetics in the presence of Cu2+ at pH 8.0 to mathematical models of amyloid formation. (ac) Normalized kinetic profiles of 2.6 µM Aβ(1-42) at pH 8.0 corresponding to the data in Figure 4. Solid lines are the global fits to data using a model for Cu2+-dependent variation in the elongation rate constant (k+). (d) Relative change in the elongation rate constant (k+) determined from the fitting of the data in (ac) compared to the relative rate determined via the linear approximation of the initial slope at 25% seeds in Figure 4e. All the rate constants are relative to that of 2.6 µM of Aβ(1-42) in the absence of Cu2+.