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. 2021 Apr 26;11:8921. doi: 10.1038/s41598-021-87959-5

Table 1.

Screening up-mutants for GFRAL binding affinity and p-ERK signaling activity.

Fc-GDF15 variant NxT mutation Up-mutation KD analysis (N = 2) Functional activity (N = 3)
hGFRAL ECD
KD (nM)
mGFRAL ECD
KD (nM)
% Intrinsic activity (Ymax) EC50 (pM)
Fc-GDF15 WT 11.0 ± 8.2E−10 230.0 ± 4.2E−08 100 177 ± 95
Mutant 2 A3N/N5T 10.0 ± 4.0E−11 245.0 ± 3.3E−08 64 ± 17 114 ± 19
Mutant 2A A3N/N5T L36H 6.03 ± 2.3E−11 186.0 ± 1.3E−08 66 ± 18 312 ± 61
Mutant 2C A3N/N5T V98I 5.52 ± 4.0E−10 95.8 ± 3.2E−09 85 ± 16 436 ± 277
Mutant 3 R4N/G6T 11.2 ± 3.7E−10 300.0 ± 8.1E−08 59 ± 18 298 ± 95
Mutant 3A R4N/G6T L36H 6.09 ± 4.5E−12 178.0 ± 2.8E−09 67 ± 15 4838 ± 2165
Mutant 3B R4N/G6T L36R 3.68 ± 8.9E−11 82.8 ± 2.0E−09 47 ± 14 4225 ± 3773
Mutant 3C R4N/G6T V98I 5.44 ± 4.0E−11 124.0 ± 4.2E−08 45 ± 12 642 ± 210

Table summarizing in vitro characteristics of Fc-GDF15 up-mutants compared to a wildtype (WT) Fc-GDF15 control. Binding affinity (KD) was measured for recombinant human and mouse GFRAL extra-cellular domain (ECD) using surface plasmon resonance (N = 2). Functional activity was measured using p-ERK HTRF assay and reported as EC50 and % intrinsic activity (Ymax) normalized to Fc-GDF15 WT (N = 3). Data are shown as mean ± SD.