**Background**
Heat shock protein 90 (Hsp90) is a highly conserved molecular chaperone that plays a critical role in the folding, stability, and maturation of numerous client proteins, many of which are oncogenic kinases and transcription factors. Due to its ability to maintain the stability of proteins essential for cell survival and proliferation, Hsp90 is frequently overexpressed in various malignancies. Consequently, the inhibition of Hsp90 leads to the degradation of these client proteins, triggering cell cycle arrest and apoptosis. Given its central role in maintaining the proteome of malignant cells, Hsp90 has become a significant target for the development of novel anticancer therapies. In this context, we will introduce a potent and selective Hsp90 inhibitor – EC144.
**Definition**
EC144 is a potent and selective inhibitor of heat shock protein 90 (Hsp90) with an IC50 value of 1.1 nM.
**In Vitro and In Vivo Studies**
According to the EC144 description, this compound is a click chemistry reagent containing an alkyne group, which allows it to undergo copper-catalyzed azide-alkyne cycloaddition (CuAAc) with molecules containing azide groups. Regarding EC144 biological activity, in vitro studies demonstrated that EC144 effectively inhibits HSP90alpha in human MCF7 cells, with an EC50 of 14 nM, as assessed by the degradation of the client protein Her-2. Furthermore, EC144 in vivo studies have shown that the compound can inhibit tumor growth and induce partial tumor regressions in animal models. These results highlight the potential of EC144 for the research of EC144 Cancer diseases. In conclusion, EC144 is a potent Hsp90 inhibitor that serves as a valuable tool for studying cancer therapy and chemical proteomics.
Keywords
EC144, 911397-80-3, EC 144, EC-144, HSP, Heat shock proteins, heat shock protein 90, tumor growth, partial tumor regressions, cancer, Inhibitor, inhibitor, inhibit
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