Fig. 2: Recombinant MIF specifically suppresses mutant SOD1 amyloid fibril formation in a dose-dependent manner | Cell Death & Disease

Fig. 2: Recombinant MIF specifically suppresses mutant SOD1 amyloid fibril formation in a dose-dependent manner

From: MIF inhibits the formation and toxicity of misfolded SOD1 amyloid aggregates: implications for familial ALS

Fig. 2: Recombinant MIF specifically suppresses mutant SOD1 amyloid fibril formation in a dose-dependent manner

ThT fluorescence was monitored during the co-incubation of SOD1G93A (50 µM) (a) or SOD1G85R (50 µM) (b) with recombinant MIF at different molar ratios at 37 °C with continuous shaking. The values were normalized to the maximal ThT intensity elicited by SOD1G93A or SOD1G85R alone. c ThT fluorescence of the β-amyloid peptide (Ab42) (1.0 µM), incubated alone or with increasing concentrations of recombinant MIF, under the same conditions as in (a) and (b). Data points in a–c represent the average results from one representative experiment (performed in triplicates) of three independent experiments. d An increase in the turbidity measured at 406 nm indicates the formation of SOD1G93A aggregates in solution during shake-incubation at 37 °C, in the absence (black) or presence (blue) of 10 μM MIF. The turbidity of MIF alone (10 μM; red) is also shown as a control. Of note, in this MIF concentration range (blue symbols) significant inhibition of ThT fluorescence elicited by SOD1G93A or SOD1G85R is seen.

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