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Updated: May 7, 2026
Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors
Published on: January 20, 2023
Targeting the hydrophobic region of Hsp90's ATP binding pocket with novel 1,3,5-triazines
1College of Pharmacy, Research Institute of Pharmaceutical Sciences, Kyungpook National University, Daegu 702-701, South Korea.
Abstract:
Heat shock protein 90 (Hsp90) is a molecular chaperone that plays an important role in regulating the maturation and stabilization of many oncogenic proteins. In an attempt to discover a new class of Hsp90 inhibitors, a series of 1,3,5-triazine compounds were rationally designed, synthesized, and their biological activities were evaluated. Compound 3b was found to degrade Hsp90's client proteins of Her2, Met and Akt and to induce the expression level of Hsp70. The binding mode of 3b in the ATP-binding site of Hsp90 was predicted by the molecular docking.
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