1321842-03-8Relevant articles and documents
Dimerization of a heat shock protein 90 inhibitor enhances inhibitory activity
Wahyudi, Hendra,Wang, Yao,McAlpine, Shelli R.
, p. 765 - 773 (2014/01/23)
Heat shock protein 90 (hsp90) accounts for 1-2% of the total proteins in normal cells and it functions as a dimer. Hsp90 behaves as a molecular chaperone that folds, assembles, and stabilizes client proteins. We have developed a novel hsp90 inhibitor, and
A small molecule that preferentially binds the closed conformation of Hsp90
Alexander, Leslie D.,Partridge, James R.,Agard, David A.,McAlpine, Shelli R.
, p. 7068 - 7071 (2012/01/13)
Described is the synthesis of three different fluorescein-tagged derivatives of a macrocycle, and their binding affinity to heat shock protein 90 (Hsp90). Using fluorescence polarization anisotropy, we report the binding affinity of these fluorescein-labeled compounds to Hsp90 in its open state and ATP-dependent closed state. We show that the compounds demonstrate a conformation-dependent preference for binding to the closed state.
