title: Investigation of ketoprofen binding to human serum albumin by spectral methods.
abstract: The binding of ketoprofen with human serum albumin (HSA) was studied by fluorescence and absorption spectroscopic methods. Quenching of fluorescence of HSA was found to be a static quenching process. At 288.15, 298.15, 308.15 and 318.15 K, the binding constants and binding sites were obtained. The effects of Cu2+, Al3+, Ca2+, Pb2+ and K+ on the binding at 288.15 K were also studied. The thermodynamic parameters, ΔH, ΔG and ΔS were got and the main sort of acting force between ketoprofen and HSA was studied. Based on the Förster's theory of non-radiation energy transfer, the binding average distance, r, between the acceptor (ketoprofen) and the donor (HSA) was calculated.
authors.affiliation: College of Chemistry, Changchun Normal University, Changchun 130032, PR China. sy_bi@sina.com
authors.forename: Shuyun
authors.initials: S
authors.lastname: Bi
authors.forename: Lili
authors.initials: L
authors.lastname: Yan
authors.forename: Yantao
authors.initials: Y
authors.lastname: Sun
authors.forename: Hanqi
authors.initials: H
authors.lastname: Zhang
mesh_terms: D006801:Humans; D006863:Hydrogen-Ion Concentration / Q000187:drug effects; D007477:Ions; D007660:Ketoprofen / Q000737:chemistry / Q000378:metabolism*; D007700:Kinetics; D008670:Metals / Q000494:pharmacology; D011485:Protein Binding / Q000187:drug effects; D012709:Serum Albumin / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D013816:Thermodynamics
chemical_list: D007477:Ions; D008670:Metals; D012709:Serum Albumin; D007660:Ketoprofen