Hsp90, short for heat shock protein 90, is a molecular chaperone that plays a key role in the conformational maturation of oncogenic signaling proteins. In addition to other molecules involved in cell cycle regulation and immune responses. It supports for the appropriately folding of other proteins, offers help in protein degradation and also stabilizes some proteins needed for tumor growth.

1. Heat shock protein 90
(Hsp90)

2. Diseases related
to Hsp90
Cancer
Alzheimer’s disease and
other neurodegenerative
diseases
Viral and bacterial infections

3. an N-terminal ATP-binding domain,
a middle co-chaperone and client-binding domain,
a C-terminal dimerization domain.

4. Types of inhibitors
Hsp90 N-terminal inhibitors1
Benzoquinone ansamycin inhibitors2
Additional synthetic Hsp90 inhibitors
Radicicol and analogous inhibitors3
4
5 Hsp90 C-terminal inhibitors

5. Hsp90 N-terminal inhibitors
Although these compounds efficiently targeted
and disrupted Hsp90 function, they were not
useful for clinical application due to their
toxicity and low stability.
Geldanamycin
Radicicol

6. Benzoquinone
ansamycin
inhibitors
17-allylamino-17-demethoxy geldanamycin
(17-AAG)
17-DMAG
17-AG
Retaspimycin (IPI 504)

7. Radicicol and
analogous
inhibitors
Ganetespib (STA-9090)
CCT018159
KW-2478
Luminespib (NVP-AUY922)
Onalespib (AT-13387)

8. Additional
synthetic Hsp90
inhibitors
Purinebased compounds
PU-H71
CNF2024/BIIB021
MPC-3100 Debio 0932
Benzamide compounds
SNX-5422/PF-04929113
SNX2112
TAS-116

9. Hsp90 C-terminal
inhibitors
Novobiocin
Epigallocatechin Gallate

10. Contact us
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