A study on the binding interaction between the imidazole derivative and bovine serum albumin by fluorescence spectroscopy

作者：Jayabharathi Jayaraman^*; Thanikachalam Venugopal; Perumal Marimuthu Venkatesh

来源：Journal of Luminescence, 2012, 132(3): 707-712.

DOI：10.1016/j.jlumin.2011.10.023

• Imidazole derivative
• Bovine serum albumin
• Synchronous fluorescence spectra
• Fluorescence quenching
• Binding studies

The interaction between the imidazole derivative 2-(2,4-difluorophenyl)-1-phenyl-1H-imidazo[4,5-f] [1,10]phenanthroline (dfppip) and bovine serum albumin (BSA) was investigated by fluorescence and UV-vis absorbance spectroscopy. From the experimental results, it was found that the imidazole derivative has strong ability to quench the intrinsic fluorescence of BSA by forming complexes. Electrostatic interactions play an important role to stabilize the complex. The binding constants and the number of binding sites have been determined in detail. The distance (r) between the donor and the acceptor was obtained according to fluorescence resonance energy transfer (FRET). Conformational changes of BSA were observed from synchronous fluorescence spectroscopy. The effect of metal ions such as Cu2+, Zn2+, Ca2+, Mg2+, Ni2+, Co2+ and Fe2+ on the binding constants between the imidazole derivative and BSA were also studied.

• 出版日期2012-3