title: [Study on the interaction between methylene blue and bovine serum albumin by fluorescence spectroscopy].
abstract: The binding characteristics of methylene blue (MB) and bovine serum albumin (BSA) has been studied by fluorescence spectroscopy in aqueous solution. The results show that the equilibrium constant KA = 3.44 x 10(5) L.mol-1, the number of binding sites n = 1.03, and the quenching mechanism of fluorescence of BSA by MB is a static quenching procedure. The binding distance between MB and BSA and the energy transfer efficiency are obtained based on the theory of Förester spectroscopy energy transfer. The effect of MB on the conformation of BSA is further analyzed using synchronous fluorescence spectrometry.
authors.affiliation: Department of Chemical Engineering, Xiangtan Polytechnic University, Xiangtan 411201, China.
authors.forename: P G
authors.initials: PG
authors.lastname: Yi
authors.forename: J F
authors.initials: JF
authors.lastname: Liu
authors.forename: Z C
authors.initials: ZC
authors.lastname: Shang
authors.forename: Q S
authors.initials: QS
authors.lastname: Yu
mesh_terms: D000818:Animals; D002417:Cattle; D004347:Drug Interactions; D004735:Energy Transfer; D008751:Methylene Blue / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D012710:Serum Albumin, Bovine / Q000737:chemistry* / Q000378:metabolism; D013050:Spectrometry, Fluorescence
chemical_list: D012710:Serum Albumin, Bovine; D008751:Methylene Blue