title: Binding interactions of pefloxacin mesylate with bovine lactoferrin and human serum albumin.
abstract: 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.
authors.affiliation: Department of Chemistry, Zhejiang University, Hangzhou 310027, China.
authors.forename: Ji-cai
authors.initials: JC
authors.lastname: Fan
authors.forename: Xiang
authors.initials: X
authors.lastname: Chen
authors.forename: Yun
authors.initials: Y
authors.lastname: Wang
authors.forename: Cheng-ping
authors.initials: CP
authors.lastname: Fan
authors.forename: Zhi-cai
authors.initials: ZC
authors.lastname: Shang
mesh_terms: 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
chemical_list: D000900:Anti-Bacterial Agents; D012709:Serum Albumin; D015366:Pefloxacin; D007781:Lactoferrin