The investigation of the interaction between ribavirin and bovine serum albumin by spectroscopic methods.
The interaction between ribavirin (RIB) with bovine serum albumin (BSA) has been investigated by fluorescence quenching technique in combination with UV-vis absorption and circular dichroism (CD) spectroscopies under the simulative physiological conditions. The quenching of BSA fluorescence by RIB was found to be a result of the formation of RIB-BSA complex. The binding constants and the number of binding sites were calculated at three different temperatures. The values of thermodynamic parameters ∆H, ∆S, ∆G at different temperatures indicate that hydrophobic and hydrogen bonds played important roles for RIB-BSA association. The binding distance r was obtained according to the theory of Förster's non-radiation energy transfer. The displacement experiments was performed for identifying the location of the binding site of RIB on BSA. The effects of common ions on the binding constant of RIB and BSA were also examined. Finally, the conformational changes of BSA in the presence of RIB were also analyzed by CD spectra and Synchronous fluorescence spectra.
College of Chemistry, Liaoning University, Shenyang, 110036, People's Republic of China. guoxja@sina.com
Xing-Jia
XJ
Guo
Ai-Jun
AJ
Hao
Xiao-Wei
XW
Han
Ping-Li
PL
Kang
Yu-Chun
YC
Jiang
Xiang-Jun
XJ
Zhang
D000818:Animals; D001665:Binding Sites; D002417:Cattle; D002942:Circular Dichroism; D004735:Energy Transfer; D007477:Ions; D007700:Kinetics; D012254:Ribavirin / Q000737:chemistry / Q000378:metabolism*; D012710:Serum Albumin, Bovine / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D013057:Spectrum Analysis / Q000379:methods*; D013696:Temperature
D007477:Ions; D012710:Serum Albumin, Bovine; D012254:Ribavirin