Table 5.
Preclinical studies of targeting other molecular chaperones
Compound | Structure | Activity | Mechanism (Sites) |
---|---|---|---|
Compound 2H | ![]() |
cIC50 = 5.0 µM | HSP110 Inhibitor (/) |
iHSP110-33 | ![]() |
bIC50 = 58 μM | HSP110 Inhibitor (NBD) |
GdnHCl | ![]() |
Kd ≈ 600 μM | ClpB Inhibitor (NTD) |
DBeQ | ![]() |
aIC50 ≈ 5.0 μM | ClpB Inhibitor (NTD) |
Mizoribine | ![]() |
/ | HSP60 inhibitor (NBD) |
ETB | ![]() |
cIC50 = 1.1 μM | HSP60 inhibitor (Cys442 covalent site) |
MC | ![]() |
/ | HSP60 inhibitor (/) |
O-carboranyl-phenoxyacetanilide | ![]() |
cIC50 = 0.74 μM | HSP60 inhibitor (NBD) |
[Au(TPP)Cl] | ![]() |
cIC50 = 1.1 μM | HSP60 inhibitor (/) |
KHS101 | ![]() |
cIC50 = 14 μM | HSP60 inhibitor (/) |
RP101 | ![]() |
/ | HSP27 inhibitor (Phe29 and Phe33) |
J2 | ![]() |
cIC50 = 99 μM | HSP27 inhibitor (Cysteine-thiol group) |
MK-933 | ![]() |
/ | HSP27 inhibitor (NTD) |
Kd target binding affinity, aIC50 ATPase inhibitor activity, bIC50 competitive binding activity, cIC50 inhibitory activity on molecular chaperone functions, “/” indicates no clear reports