Heat shock protein 90 (Hsp90) is an often-mentioned molecular chaperone. Heat shock protein 90 (Hsp90) exerts an important role in the maturation and stability of client proteins. Oncogenic client proteins, which are the target molecules of many anticancer compounds, and encompass dysregulated, mutated, and fusion proteins, are particularly dependent on Hsp90 for maintaining their conformation.
17-allylamino,17-demethoxygeldanamycin (17-AAG) is a novel anticancer drug that is a less toxic analogue of the geldanamycin which binds to Hsp90 and alters its function. HSP90 client proteins play important roles in the regulation of the cell cycle, cell growth, cell survival, apoptosis, and oncogenesis.
Ansamycins is a family of secondary metabolites that show antimicrobial activity against many gram-positive and some gram-negative bacteria and includes various compounds, among which: streptovaricins and rifamycins. In addition, these compounds demonstrate antiviral activity towards bacteriophages and poxviruses.