Functional characterization of heat shock protein 90 targeted compounds.
|Title||Functional characterization of heat shock protein 90 targeted compounds.|
|Publication Type||Journal Article|
|Year of Publication||2013|
|Authors||Cruz IN, Zhang Y, de la Fuente M, Schätzlein A, Yang M|
|Date Published||2013 Jul 15|
|Keywords||Adenosine Triphosphatases, Antineoplastic Agents, Biological Assay, HSP90 Heat-Shock Proteins, Inhibitory Concentration 50, Protein Binding|
Heat shock protein 90 (Hsp90) is an attractive cancer target that possesses two potential binding domains at the C and N termini. Nevertheless, assays that can reliably distinguish between the C- and N-terminal Hsp90 inhibitors and quantitatively characterize candidate drugs are limited. Here we report an Hsp90 binding assay and ATPase inhibition assay that can not only separate the C- and N-terminal inhibitors but also quantitatively determine their respective IC50 values.
|Alternate Journal||Anal. Biochem.|