Study on the Interaction between Human Serum Albumins and Methyl Pheophorbide-a-Gd

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 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 Forsters 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 Ⅱ of HSA.

关键词： methyl pheophorbide-a-Gd Human Serum Albumins fluorescence quenching binding reaction rare earths

作者: Li Guizhi (李桂芝) Liu Yongming (刘永明)

作者单位: College of Chemistry, Yantai University, Yantai 264005, China

会议类型: 国际会议

会议名称: 第五届国际稀土开发与应用研讨会(The Fifth International Conference on Rare Earth Decelopment and Applicatin)

会议地点: 包头

会议语种:英文

页码: 338-341

在线出版日期: 2007-08-07（万方平台首次上网日期，不代表论文的发表时间）