HSP90 inhibitors: current development and potential in cancer therapy

[bocsci11]

In the last decade, the molecular chaperone HSP90 has emerged as an important target in cancer therapeutics and has subsequently become the focus of several drug discovery and development efforts. The first-in-class HSP90 inhibitor 17-AAG entered into Phase I clinical trial in 1999. Today 13 HSP90 inhibitors representing multiple drug classes, with different modes of action, are undergoing clinical evaluation.

Hsp90 is the most abundant heat shock protein and represents 1-2% of total cellular proteins in unstressed cells. It is unique from the other chaperones in that it does not play a major role in de novo polypeptide folding. Instead, it regulates post-translational maturation of many conformationally unstable substrates or client proteins, many of which are involved in oncogenesis.

[Johnjohn20]

Health

[AllanNawyer]

HSP90 inhibitors have indeed made significant strides in cancer therapy over the past decade, showing great promise in targeting various oncogenic processes. As research continues, it's exciting to see how these inhibitors evolve and how they might integrate into broader therapeutic strategies.

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[halealex]

HSP90 inhibitors are a promising area in cancer therapy, targeting the molecular chaperone HSP90 to disrupt cancer-related proteins. Since the first-in-class inhibitor 17-AAG entered trials in 1999, multiple HSP90 inhibitors with different company mechanisms are in clinical evaluation. These inhibitors help regulate oncogenic proteins by interfering with HSP90’s role in post-translational protein maturation.