Digital Commons Network^™

Stimulation Of Heat Shock Protein 90 Chaperone Function Through Binding Of A Novobiocin Analog Ku-32, Bhaskar K. Chatterjee, Abhilash Jayaraj, Vinay Kumar, Brian Blagg, Rachel E. Davis, B Jayaram, Shashank Deep, Tapan K. Chaudhuri

Faculty Publications

Heat shock protein 90 (Hsp90) is a eukaryotic chaperone responsible for the folding and functional activation of numerous client proteins, many of which are oncoproteins. Thus, Hsp90 inhibition has been intensely pursued, resulting in the development of many potential Hsp90 inhibitors, not all of which are well-characterized. Hsp90 inhibitors not only abrogate its chaperone functions, but also could help us gain insight into the structure-function relationship of this chaperone. Here, using biochemical and cell-based assays along with isothermal titration calorimetry, we investigate KU-32, a derivative of the Hsp90 inhibitor novobiocin (NB), for its ability to modulate Hsp90 chaperone function. Although …