Study on the Interaction between Cisplatin and Bovine Serum Albumin by Fluorescent Spectrometry / 中国药师

Objective:To study the interaction between cisplatin and bovine serum albumin ( BSA) under the simulated human physiological condition. Methods:The interaction mechanism of BSA and cisplatin was investigated by fluorescent spectrometry; the binding constant, binding site and interaction force were studied, and the interaction effects on the conformation change of BSA were investigated as well. Results:The results of fluorescent spectrometry showed that a ground state complex was formed between cisplatin and BSA, and the mechanism of fluorescence quenching was static quenching. The binding parameters of cisplatin and BSA were as follows:the binding constant was 1. 36 × 104 L·mol-1 , the binding site was 0. 991, and the interaction was mainly driven by hydrogen bonds and Van Der Waals forces. The results of synchronous fluorescent spectrometry demonstrated that the interaction influenced the micro-environments of amide acid residues. Conclusion:Cisplatin can interact with BSA and change the conformation of BSA.

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

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.

Study on pharmacokinetics of PSD-007 in BN rats by fluorescence detection methods / 国际生物医学工程杂志

Objective To investigate the pharmacokinetic characteristics of PSD-007 in BN rats.Methods Blood of the BN rats was collected from the inner canthus after iv administration of PSD-007,and the plasma drug concentrations at different times were determined by fluorescent spectrometry.The best compartment model and the pharmacolinetic were calculated by the software of DNS 2.0.Results The elimination process of PSD-007 fitted three-compartment open model after iv administration.The principal pharmacokinetic parameters were t1/2α=0.096 h,t1/2β=1.299 h,t12γ=19.387 h,V1=0.259 L/kg,A UC=15.263 mg/(L ·h).Conclusions The sensitivity of fluorescent spectrometry was high and the operation is sinple and the progress is short.PSD-007 has fast absorption,quick effect and elimination without accumulation phenomenon.