Table 1.
Physicochemical properties of the optimized de novo miniprotein binders
| H3 | TrkA | FGFR2 | EGFRn | EGFRc | PDGFR | IR | IGF1R | TIE2 | IL-7Rα | CD3δ | TGFβ | VirB8 | |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Kd (nM) | 320 ± 24.0 | 1.4 ± 0.02 | 243 ± 59.0 | 1.2 ± 0.01 | 6.8 ± 0.3 | 82 ± 25 | 210 ± 39 | 860 ± 270 | 584 ± 35 | 0.31 ± 0.004 | 612 ± 30 | 113 ± 4.4 | 0.51 ± 0.005 |
| TM (°C) | > 95.0 | > 95.0 | 71.1 | > 95.0 | 71.2 | > 95.0 | 65.0 | > 95.0 | > 95.0 | > 95.0 | > 95.0 | > 95.0 | 66.2 |
The binding affinity and melting temperature (TM) of the optimized de novo miniprotein binders. See Figs. 2 and 3 for the circular dichroism spectra; the raw biolayer interferometry traces are in Extended Data Fig. 4. Experimental details can be found in the corresponding figure legends and section of the Methods.