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- W994780293 abstract "The binding reaction between camptothecin derivatives, such as 7-Ethylcamptothecin (7-ECPT) and 10-hydroxycamptothecin (10-HCPT), and bovine serum albumins (BSA) were studied by fluorescence and ultraviolet-visible absorption spectrometry. The research results indicate that the combination reaction of them is a single static quenching process, camptothecin derivatives strongly bind BSA with the molar ratio of 1:1, the binding equilibrium constants (K0) are as follows, K(subscript 0,7-ECPT)=3.69×10^5 L/mol, K(subscript 0,10-HCPT)=8.00×10^5 L/mol. The shortest binding distance (r) and energy transfer efficiencies (E) between donor (BSA) and acceptor (camptothecin derivatives) were obtained by Forster's nonradiative energy transfer mechanism, the shortest binding distance (r) and energy transfer efficiencies (E) are as follows, r(subscript 7-ECPT)=3.03 nm, r(subscript 10-HCPT)=3.27 nm; E(subscript 7-ECPT)=0.48, E(subscript 10-HCPT)=0.31. The main sort of binding force between them is hydrophobic force." @default.
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- W994780293 date "2006-09-01" @default.
- W994780293 modified "2023-09-23" @default.
- W994780293 title "荧光法研究7-乙基喜树碱、10-羟基喜树碱和牛血清白蛋白的相互作用" @default.
- W994780293 hasPublicationYear "2006" @default.
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