Interactions study between C0817 and Hsp90 by fluorescence spectrometry / 中国药学杂志

ABSTRACT

OBJECTIVE: To estimate the interaction between C0817 and Hsp90 and the inhibitory effects C0817 on the activity Hsp90 ATPase. METHODS: The fluorescent spectrometry method was applied to examine the affinity between different concentrations C0817 and Hsp90; fluorescence intensities were recorded in the range 290-510 nm at 293 K, 303 K and 310 K, respectively; colori-metric assay for inorganic phosphate based on the formation a phosphomolybdate complex and subsequent reaction with malachite green was used to examine the inhibitory effects C0817 on the activity Hsp90 ATPase. RESULTS: The dissociation constant KD value C0817 was (24.740 ± 1.752) μmol · L-1. The interaction between C0817 and Hsp90 was driven mainly by electrostatic interaction. When the concentration ATP was 1 mmol · L-1, C0817 could not inhibit the ATPase activity Hsp90. CONCLUSION: The interaction mechanism between C0817 and Hsp90 can be analyzed by fluorescence spectrum. C0817 doesn't show inhibitory action for ATPase Hsp90.