Table 2.
Enzyme inhibition activities from ten-point dose response assays of selected resynthesized electrophilic fragments at caspase-2 and caspase-3.
| pIC50 ± SEMa | |||||
|---|---|---|---|---|---|
| Cmpd. | Casp2 | N | Casp3 | N | IC50 („cmp“ @Casp2) / IC50 („cmp*“@Casp2) |
|
| |||||
| AcVDVAD-CHO b | 7.32 ± 0.01d | 3 | n.d. | - | - |
| AcDEVD-CHO c | n.d. | - | 8.86 ± 0.01 | 3 | - |
| 17* | 5.48 | 1 | n.d. | - | 3.06 |
| 97* | 5,31 ± 0.01d | 3 | < 4.50 | 3 | 2.64 |
| 97** | 5.47 | 1 | n.d. | - | 1.85 |
| 1269* | 5,22 ± 0.01d | 3 | < 4.50 | 3 | 1.89 |
| 1921 | 5.27 | 2 | n.d. | - | - |
a
pIC50 values were obtained based on measurements at 40 min. Data shown are mean values ± SEM of N independent experiments, each performed in duplicate. Data were analyzed by nonlinear regression and were best fitted to sigmoidal concentration-response curves (variable slope, four parameter fit).
b
AcVDVAD-CHO was used as a reference compound against caspase-2.
c
AcDEVD-CHO was used as a reference compound against caspase-3.
d
Assayed with cpCasp2.[23]