Binding interactions of pefloxacin mesylate with bovine lactoferrin and human serum albumin.
The binding of pefloxacin mesylate (PFLX) to bovine lactoferrin (BLf) and human serum albumin (HSA) in dilute aqueous solution was studied using fluorescence spectra and absorbance spectra. The binding constant K and the binding sites n were obtained by fluorescence quenching method. The binding distance r and energy-transfer efficiency E between pefloxacin mesylate and bovine lactoferrin as well as human serum albumin were also obtained according to the mechanism of Förster-type dipole-dipole nonradiative energy-transfer. The effects of pefloxacin mesylate on the conformations of bovine lactoferrin and human serum albumin were also analyzed using synchronous fluorescence spectroscopy.
Fan
Ji-cai
JC
Department of Chemistry, Zhejiang University, Hangzhou 310027, China.
Chen
Xiang
X
Wang
Yun
Y
Fan
Cheng-ping
CP
Shang
Zhi-cai
ZC
D000818:Animals; D000900:Anti-Bacterial Agents / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology; D001665:Binding Sites; D002417:Cattle; D006801:Humans; D007700:Kinetics; D007781:Lactoferrin / Q000737:chemistry / Q000378:metabolism*; D015366:Pefloxacin / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology; D011485:Protein Binding; D011487:Protein Conformation; D012709:Serum Albumin / Q000737:chemistry / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet
D000900:Anti-Bacterial Agents; D012709:Serum Albumin; D015366:Pefloxacin; D007781:Lactoferrin