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Hsp90 inhibitors are a group of drugs that inhibit the function of Hsp90, a protein that plays a key role in cell signaling, proliferation, and survival. Hsp90 inhibitors are being studied for their potential use in the treatment of cancer and other diseases.

Function of Hsp90

Hsp90 is a chaperone protein that assists other proteins to fold properly, stabilizes proteins against heat stress, and aids in protein degradation. It also stabilizes a number of proteins required for tumor growth, which is why Hsp90 inhibitors are being studied as potential anti-cancer drugs.

Mechanism of action

Hsp90 inhibitors work by binding to the ATP-binding pocket of Hsp90, thereby inhibiting its chaperone function. This leads to the degradation of proteins that require Hsp90 for folding and stability, many of which are involved in cell growth and proliferation.

Types of Hsp90 inhibitors

There are several types of Hsp90 inhibitors, including Geldanamycin, Radicicol, and synthetic inhibitors such as 17-AAG, 17-DMAG, and IPI-504. These inhibitors differ in their specificity for Hsp90 and their ability to cross the blood-brain barrier.

Clinical applications

Hsp90 inhibitors are being studied in clinical trials for the treatment of various types of cancer, including breast cancer, lung cancer, and melanoma. They are also being investigated for their potential use in the treatment of neurodegenerative diseases such as Alzheimer's disease and Parkinson's disease.

Side effects

Like all drugs, Hsp90 inhibitors can have side effects. These can include nausea, vomiting, diarrhea, and fatigue. More serious side effects can include liver damage and cardiac toxicity.

See also

• Heat shock protein
• Cancer treatment
• Neurodegenerative disease