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Investigation of the binding behavior of human serum albumin and phosphorothioate oligodeoxynucleotide

Guo-Zhu Ye, Liang-Ren Zhang*, Li-He Zhang   

  1. State Key Laboratory of Natural and Biomimetic Drugs, School of Pharmaceutical Sciences, Peking University, Beijing 100083, China
  • Received:2006-11-10 Revised:2007-02-10 Online:2007-03-15 Published:2007-03-15
  • Contact: Liang-Ren Zhang*

Abstract: 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) Zn2+ and Ni2+ 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 role in the interaction.

Key words: Phosphorothioate oligodeoxynucleotide, Phosphorothioate oligodeoxynucleotide, Human serum albumin, Human serum albumin, Positive potential region, Positive potential region, Conformational changes, Conformational changes

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