Figure 4
(a) Aggregation kinetics of MAK33 VL S20N induced by EGCG. 1H NMR was employed for quantification. (b) Precipitation of the VL variants with altered EGCG binding properties in presence of a 10-fold molar excess of EGCG. (c) The more amyloidogenic mutants D70N and I2E precipitate faster in presence of a 10-fold excess of EGCG, although D70N has the same thermodynamic stability as the WT. (d) Thermal unfolding of MAK33 VL P44A and P59A. The mutations do not affect melting temperatures, as confirmed by CD thermal transitions. (e) ThT fibril formation assays for VL I2E with and without EGCG. (f) EGCG to protein VL S20N molar ratio in the aggregates quantified by 1H NMR signal intensities.
