Heat shock proteins 90 as a novel target for cancer therapy

Heat shock proteins 90 (HSP90) is essential for the maintenance of appropriate folding and conformation of many cell signaling proteins, which are involved in cell proliferation and survival and already several HSP90 inhibitors are under clinical evaluation 1 . A major attraction of HSP90 inhibitors is their potential to inhibit a range of oncogenic client proteins and cancer pathways, thereby blocking all of the ‘hallmark traits’ of cancer and exhibiting broad-spectrum antitumor activity 2 . Many studies have suggested that targeting of the HSP90 molecular chaperone has great potential for cancer therapy 1 .