Investigation of the binding behavior of human serum albumin and phosphorothioate oligodeoxynucleotide
人血清白蛋白与硫代寡核苷酸的结合研究作者机构:北京大学药学院天然药物及仿生药物国家重点实验室北京100083
出 版 物:《Journal of Chinese Pharmaceutical Sciences》 (中国药学(英文版))
年 卷 期:2007年第16卷第1期
页 面:9-13页
学科分类:1007[医学-药学(可授医学、理学学位)] 10[医学]
基 金:This work was supported by the National Natural Science Foundation of China(20472007)
主 题:Phosphoruthioate oligodeoxynucleotide Human serum albumin Positive potential region Conformational changes
摘 要:Aim To study the binding behavior between human serum albumin (HSA) and phosphorothioate oligodeoxynucleotide (PS- ODN) and the effects of bivalent cations on the interaction. Methods Surface plasma resonance, circular dichroism and fluorescence experiments were conducted. Results ( 1 ) the binding ability was decreased along with the increase of pH; (2) Zn^2+and Ni^2+ enhanced the interaction between PS-ODN and HSA; (3) Upon PS-ODN binding, the conformation of HSA was changed with an increase of β - sheet. Conclusion The results provide experimental evidences to the hypothesis that PS-ODN binds with HSA in the positive potential region, and histidine residues located in the region play a crucial rule in the interaction.