Nuclear Science and Techniques

《核技术》(英文版) ISSN 1001-8042 CN 31-1559/TL     2019 Impact factor 1.556

Nuclear Science and Techniques ›› 2015, Vol. 26 ›› Issue (3): 030505 doi: 10.13538/j.1001-8042/nst.26.030505

• NUCLEAR PHYSICS AND INTERDISCIPLINARY RESEARCH • Previous Articles     Next Articles

Fluorimetric study on the interaction between fluoresceinamine and bovine serum albumin

LIU Yu-Shuang, ZHANG Ping, ZHONG Rui-Bo, BAI Zhi-Jun, GUO Jun, ZHAO Guo-Fen, and ZHANG Feng   

  1. School of Life Science, Inner Mongolia Agricultural University, 306 Zhaowuda Road, Hohhot 010018, China
  • Contact: ZHANG Feng E-mail:fengzhang1978@hotmail.com
  • Supported by:

    Supported by National Natural Science Foundation of China (Nos. 21171086 and 81160213), the Inner Mongolia Grassland Talent (No. 108-108038), the Inner Mongolia Autonomous Region Natural Science Foundation (No. 2013MS1121), and the Inner Mongolia Agricultural University (Nos. 211-109003 and 211-206038)

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LIU Yu-Shuang, ZHANG Ping, ZHONG Rui-Bo, BAI Zhi-Jun, GUO Jun, ZHAO Guo-Fen, and ZHANG Feng. Fluorimetric study on the interaction between fluoresceinamine and bovine serum albumin.Nuclear Science and Techniques, 2015, 26(3): 030505     doi: 10.13538/j.1001-8042/nst.26.030505

Abstract:

Fluorescence spectroscopy was employed to investigate the interaction between fluorophore fluoresceinamine (FA) and bovine serum albumin (BSA) under physiological conditions. In the mechanism discussion, it was proved that the fluorescence quenching of BSA by FA is a result of the formation of a BSA-FA complex. Fluorescence quenching constants were determined using the modified Stern-Volmer equation to provide a measure of the binding affinity between FA and BSA. The results of the thermodynamic parameters ?G, ?H, and ?S at different temperatures indicated that several kinds of interactions, except for the electrostatic interactions play cooperative roles in BSA-FA association. Furthermore, the conformation of BSA upon interaction with FA was also studied by synchrotron fluorescence spectroscopy.

Key words: Bovine serum albumin, Fluoresceinamine, Fluorescence quenching, Binding constant, Protein conformation