Acta Chimica Sinica ›› 2007, Vol. 65 ›› Issue (21): 2417-2422. Previous Articles     Next Articles



  1. (1安阳师范学院化学系 安阳 455002)
    (2郑州大学化学系 河南省化学生物与有机化学重点实验室 郑州 450052)
    (3中国药科大学中药现代化重点实验室 南京210038)
  • 投稿日期:2007-01-12 修回日期:2007-06-11 发布日期:2007-11-14
  • 通讯作者: 屈凌波

Study on the Interaction of Bovine Serum Albumin with Puerarin and Its Derivatives

QU Ling-Bo*,1,2; WANG Ling 2; CHEN Xiao-Lan2; YUAN Jin-Wei 2; YANG Ran2; LI Ping 3   

  1. (1 Department of Chemistry, Anyang Normal College, Anyang 455002)
    (2 Key Laboratory for Bio-Chemistry and Organic Chemistry of Henan Province, Department of Chemistry, Zhengzhou University, Zhengzhou 450052)
    (3 Key Laboratory of Modernization of Chinese Traditional Medicine, China Pharmaceutical University, Nanjing 210038)
  • Received:2007-01-12 Revised:2007-06-11 Published:2007-11-14
  • Contact: QU Ling-Bo

In the paper, two new phosphorylated isoflavones of puerarin were successfully obtained by a modified Atheron-Todd reaction. Further, the interactions of bovine serum albumin (BSA) and puerarin or its phosphorylated products were studied under physiological pH by fluorescence spectroscopy. The results showed that puerarin and its phosphorylated products all could form a non-covalent complex with BSA, while the interactions of the phosphorylated isoflavones with BSA were weaker than puerarin. The quench-ing mechanisms of them with BSA were suggested as a static quenching process, and the binding force was mainly a hydrophobic force. The distances between BSA and puerarin and its phosphorylated isoflavones were less than 7 nm according to the theory of the Förster energy transference. The relationship between the molecule structures of these compounds and the binding ability of them with BSA was preliminarily dis-cussed, and the quenching constants in the presence of various metal ions were also explored.

Key words: fluorescence spectroscopy, puerarin, phosphorylation, bovine serum albumin