[Fluorescence study on the interaction of salicylic acid and bovine serum albumin].
The interaction between salicylic acid and bovine serum albumin has been studied by fluorescence spectroscopy. The results show that the quenching mechanism of the combination of bovine serum albumin with salicylic acid is a static quenching procedure, the quenching constant K(sv) is 1.097 x 10(4) (mol x L(-1))(-1), and the equilibrium constant is 7.377 x 10(4). The number of binding sites is 1 and it is a strong one. When the ratio of molar concentration of salicylic acid to bovine serum albumin is lower than 1:1, it binds to Trp residue first but it doesn't result in any microenvironment changes of Trp residue. The binding distance between salicylic acid and bovine serum albumin and the energy transfer efficiency were obtained based on the theory of Förester spectroscopy energy transfer.
Xiao
Hou-rong
HR
Department of Chemistry, University of Science and Technology of China, Hefei, China.
Sheng
Liang-quan
LQ
Shi
Chun-hua
CH
Xu
Xiao-long
XL
Xie
Yong-shu
YS
Liu
Qing-liang
QL
D001665:Binding Sites; D002942:Circular Dichroism / Q000379:methods; D004347:Drug Interactions; D004735:Energy Transfer; D005453:Fluorescence; D011485:Protein Binding; D011487:Protein Conformation; D020156:Salicylic Acid / Q000737:chemistry*; D012709:Serum Albumin / Q000737:chemistry*; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013050:Spectrometry, Fluorescence / Q000379:methods*; D017550:Spectroscopy, Fourier Transform Infrared / Q000379:methods
D012709:Serum Albumin; D012710:Serum Albumin, Bovine; D020156:Salicylic Acid