[Spectroscopic study on binding of indomethacin to bovine serum albumin].
The interaction between indomethacin (IM) and bovine serum albumin (BSA) under physiological condition was studied using fluorescence and absorption spectra. It was proved that fluorescence quenching of BSA by IM is deduced by combining static quenching with nonradiative energy transfer. The binding constants were obtained by fluorescence quenching method. The main sorts of binding force were determined according to the thermodynamic parameters. The binding distances and energy transfer efficiencies between indomethacin and bovine serum albumin were obtained based on the theory of Forster nonradiative energy transfer. Combining the results of UV absorption and fluorescence spectroscopic methods, the binding mode of IM with BSA was discussed.
Cao
Xi-min
XM
Center of Analysis and Test, Shanxi Normal University, Linfen 041004, China.
Du
Li-ming
LM
D000818:Animals; D002417:Cattle; D007213:Indomethacin / Q000032:analysis* / Q000737:chemistry; D015394:Molecular Structure; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013050:Spectrometry, Fluorescence / Q000379:methods*; D013053:Spectrophotometry / Q000379:methods*; D013816:Thermodynamics
D012710:Serum Albumin, Bovine; D007213:Indomethacin