TABLE 2.
Effects of compound 14 and analogs on ATPase activitya
| Compound | IC50 (μM) for ATP hydrolysis |
|||
|---|---|---|---|---|
| S. cerevisiae Pma1 | C. albicans Pma1 | Na+,K+-ATPase | SERCA | |
| 14 | 13.7 ± 2.0 | 17.0 ± 0.9 | 18.4 ± 2.1 | 42.0 ± 8.0 |
| 15 | 5.9 ± 0.2 | 6.3 ± 0.5 | 4.1 ± 0.6 | 4.5 ± 0.0 |
| 16 | 7.8 ± 0.6 | 9.5 ± 1.0 | 9.1 ± 1.0 | 11.1 ± 0.0 |
| 17 | 106.7 ± 18.2 | 150.7 ± 6.2 | >333 | >333 |
| 18 | 18.5 ± 4.3 | 22.9 ± 2.0 | 85.7 ± 26.6 | 69.5 ± 6.9 |
| 19 | 7.3 ± 1.0 | 8.7 ± 0.5 | 5.5 ± 1.8 | 4.4 ± 0.3 |
| BM2 | 1.2 ± 0.1 | 0.9 ± 0.2 | 10.4 ± 2.7 | 1.1 ± 0.0 |
| Vanadate | 0.25 ± 0.01 | 0.23 ± 0.05 | 0.006 ± 0.001 | 10.4 ± 2.4 |
| Ebselen | 0.92 ± 0.15 | 0.51 ± 0.04 | 0.16 ± 0.01 | 0.12 ± 0.00 |
a
Experiments were performed at pH 7, and standard deviations (n = 2) are given. Rabbit Ca2+-ATPase (SERCA1a) and porcine kidney Na+,K+-ATPase were used.