title: Functional characterization of heat shock protein 90 targeted compounds.
abstract: 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.
authors.affiliation: Department of Pharmaceutical and Biological Chemistry, UCL School of Pharmacy, London WC1N 1AX, UK.
authors.forename: Isa N
authors.initials: IN
authors.lastname: Cruz
authors.forename: Yixi
authors.initials: Y
authors.lastname: Zhang
authors.forename: Maria
authors.initials: M
authors.lastname: de la Fuente
authors.forename: Andreas
authors.initials: A
authors.lastname: Schatzlein
authors.forename: Min
authors.initials: M
authors.lastname: Yang
mesh_terms: D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors*; D000970:Antineoplastic Agents / Q000737:chemistry* / Q000494:pharmacology; D001681:Biological Assay / Q000379:methods*; D018841:HSP90 Heat-Shock Proteins / Q000737:chemistry*; D020128:Inhibitory Concentration 50; D011485:Protein Binding
chemical_list: D000970:Antineoplastic Agents; D018841:HSP90 Heat-Shock Proteins; D000251:Adenosine Triphosphatases