Table 1. . Calcium calmodulin serine/threonine kinase IIδ inhibitors in cardiac muscle.
No. | Structure | Inhibitor class | Study year | Activity IC50 |
---|---|---|---|---|
1 | ![]() |
Natural | 2012 | 112 µM |
2 | ![]() |
Semisynthetic | 2012 | 1.49 µM |
3 | ![]() |
Synthetic | 1990 | 500 nM |
4 | ![]() |
Synthetic | 1996 | 1.57 µM |
5 | ![]() |
Group of aryl indolyl–maleimide scaffold, synthetic inhibitors | 2008 | 10 nM to >20 µM |
6 | ![]() |
Most active aryl indolyl–inhibitor against CaMK IIδ | 2008 | 10 nM |
7 | ![]() |
Synthetic | 2012 | 12 nM |
8 | ![]() |
Homology modeling synthesis of pyrimidine-based inhibitors | 2008 | 0.009–3 µM |
9 | ![]() |
Most active pyrimidine-based inhibitor | 2008 | 9 nM |
10 | ![]() |
Synthetic | 2012 | 2 nM |
11 | ![]() |
Inhibitor resulted from ligand-based virtual screening CaMK IIδ inhibitor | 2011 | 20 nM |
12 | ![]() |
Inhibitor resulted from ligand-based virtual screening CaMK IIδ inhibitor | 2011 | 82 nM |
CaMK-IIδ: Calcium calmodulin serine/threonine kinase IIδ.