Study on the Interaction between Human Serum Albumins and Methyl Pheophorbide-a-Gd
来源期刊：Journal of Rare Earths2007年第S1期
论文作者：李桂芝 刘永明
文章页码：338 - 341
摘 要：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 single static quenching process, MPA-Gd strongly bound HSA, the binding equilibrium constant K0=2.298×105 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 Frster′s nonradiative energy transfer mechanism as follows: r=4.03 nm, E=0.12. The enthalpy change （ΔH） and entropy change （ΔS） 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 Ⅱof HSA.
李桂芝，刘永明
摘 要：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 single static quenching process, MPA-Gd strongly bound HSA, the binding equilibrium constant K0=2.298×105 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 Frster′s nonradiative energy transfer mechanism as follows: r=4.03 nm, E=0.12. The enthalpy change （ΔH） and entropy change （ΔS） 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 Ⅱof HSA.
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