Acta Chimica Sinica ›› 2007, Vol. 65 ›› Issue (1): 43-48. Previous Articles     Next Articles

Original Articles


王华芳1, 李文友1, 何锡文*,1, 陈朗星1, 张玉奎*,1,2   

  1. (1南开大学化学系 天津 300071)
    (2中国科学院大连化学物理研究所 大连 116011)
  • 收稿日期:2006-05-09 修回日期:2006-08-23 出版日期:2007-01-14 发布日期:2007-01-14
  • 通讯作者: 何锡文

Investigations of the Interaction between 3-Aminophenylboronic Acid and Bovine Serum Albumin Using Fluorimetry

WANG Hua-Fang1; LI Wen-You1; HE Xi-Wen*,1; CHEN Lang-Xing1; ZHANG Yu-Kui*,1,2   

  1. (1 Department of Chemistry, Nankai University, Tianjin 300071)
    (2 Dalian Institute of Chemical Physics, Dalian 116011)
  • Received:2006-05-09 Revised:2006-08-23 Online:2007-01-14 Published:2007-01-14
  • Contact: HE Xi-Wen

In order to understand the chemical mechanism and optimal conditions of the molecular imprinting, the interaction between 3-aminophenylboronic acid (APBA) and bovine serum albumin (BSA) was investigated using fluorescence quenching method with many factors, as the pH value, ionic strength and others, which maybe influence the interaction. The research results indicate that under appropriate ionic strength and pH 6.25, the fluorescence quenching shows that APBA strongly bound with the tryptophan of BSA, and the complex was formed with a molar ratio of 2∶1. Their apparent binding constant is KA=1.0×1011 L2•mol-2, so their chemical bonds between donor BSA and acceptor APBA are relatively strong. According to the results, the interaction mechanism between APBA and BSA is predicted. During following research, it will be entirely possible to separate or enrich BSA composition, maybe it could improve imprinting and eluting efficiency greatly.

Key words: 3-aminophenylboronic acid, bovine serum albumin, fluorescence quenching, molecularly imprinting