Table 2.
Comparation of PVTX-405 (16a), 16b and DKY709
 | ||||
|---|---|---|---|---|
| Compound | DKY709 | 16a (PVTX-405) | 16b | |
| CRBN bindinga | IC50 (nM) | 496 | 99 | 1335 |
| IKZF2 degradationb | DC50 (Dmax) | 1.5 nM (73%) | 0.7 nM (91%) | 4.1 nM (89%) |
| IKZF1 degradationb | DC50 (Dmax) | >10 µM (14%) | >10 µM (11%) | >10 µM (7%) |
| IKZF3 degradationb | DC50 (Dmax) | >10 µM (20%) | >10 µM (17%) | >10 µM (9%) |
| SALL4 degradationb | DC50 (Dmax) | 4.9 nM (55%) | >1000 nM (33%) | >1000 nM (27%) |
| GSPT1 degradationb | DC50 (Dmax) | >10 µM (16%) | >10 µM (14%) | >10 µM (13%) |
| CK1α degradationb | DC50 (Dmax) | >10 µM (15%) | >10 µM (10%) | >10 µM (7%) |
| hERG inhibitionc | IC50 (µM) | 9.0 | 48 | NT |
aTested by HTRF binding assay.
bTested by HiBiT degradation assay.
chERG inhibition was evaluated by manual patch-clamp system. All the data are presented as mean of at least two biological replicates. Source data are provided as a Source Data file.