[Studies on the reaction of balofloxacin with bovine serum albumin].
In the present paper, a fluorescence method was used to study at different pH the fluorescence quenching of bovine serum albumin (BSA) by its interaction with balofloxacin (BLFX). The interaction association constants of BSA and BLFX were determined from a double reciprocal line Weaver-Burk plot. According to the Forster dipole-dipole energy transfer, the distance to be measured between the BLFX and tryptophane is 5.09 nm. From thermodynamical coordination it can be judged that the binding power between BLFX and BSA is electrostatic effect. The effect of BLFX on the conformation of BSA was also analyzed by using synchronous fluorescence spectroscopy.
Yan
Zheng-Yu
ZY
China Pharmaceutical University, Nanjing 210009, China.
Shao
Xiu-Fen
XF
Jiang
Xin-Min
XM
Hu
Yu-Zhu
YZ
D000818:Animals; D002417:Cattle; D004735:Energy Transfer; D005453:Fluorescence; D024841:Fluoroquinolones / Q000737:chemistry* / Q000378:metabolism; D007700:Kinetics; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000737:chemistry* / Q000378:metabolism; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet; D055672:Static Electricity; D013816:Thermodynamics
D024841:Fluoroquinolones; D012710:Serum Albumin, Bovine; C077155:balofloxacin