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《Proceedings of the Fifth International Conference on Rare Earth Development and Application》 2007年
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Study on the Interaction between Human Serum Albumins and Methyl Pheophorbide-a-Gd

李桂芝  刘永明  
【摘要】:正The binding reaction between methyl pheophorbide-a-Gd(MPA-Gd)and Human Serum Albumins(HSA)was studied by fluorescence and UV-Vis absorption spectra.The results indicated that the binding reaction of them was a sin- gle static quenching process,MPA-Gd strongly bound HSA,the binding equilibrium constant K_0=2.298×10~5 L·mol~(-1) at 25℃.The shortest binding distance(r)and energy transfer efficiency(E)between donor(HSA)and acceptor(MPA- Gd)was obtained by F(?)rster's nonradiative energy transfer mechanism as follows:r=4.03 nm,E=0.12.The enthalpy change(△H)and entropy change(△S)were calculated at 25 and 37℃.The results indicated that the hydrogen bonds played major role in the reaction.Furthermore,the displacement experiments indicated that MPA-Gd could bind to the site Ⅱ of HSA.

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