title: [Study on the interaction of methyl pheophorbide-a and bovine serum albumins by fluorescence].
abstract: The binding reaction of methyl pheophorbide-a with bovine serum albumins (BSA) in aqueous solution was studied by fluorescence and UV-Vis absorption spectra. The results indicated that the combination reaction of them was a single static quenching process. In aqueous solution, methyl pheophorbide-a strongly bound BSA with the apparent molar ratio of 2 : 1 because of methyl pheophorbide-a polymerized by itself. The binding constant KB was 6.7 x 10(4) L x mol(-1). In mixture solvent of tetrahydrofuran and water, methyl pheophorbide-a existed as single molecule and bound BSA with a molar ratio of 1: 1. There is single position for combining methyl pheophorbide-a with BSA. The shortest binding distance (r = 3.50 nm) and energy transfer efficiencies (E = 0.39) between donor (BSA) and acceptor (methyl pheophorbide-a) were obtained by Förster's nonradiative energy transfer mechanism.
authors.affiliation: College of Chemistry, Yantai University, Yantai 264005, China.
authors.forename: Yong-Ming
authors.initials: YM
authors.lastname: Liu
authors.forename: Jin-Jun
authors.initials: JJ
authors.lastname: Wang
authors.forename: Xu-Ran
authors.initials: XR
authors.lastname: Wu
mesh_terms: D000465:Algorithms; D000818:Animals; D002417:Cattle; D002734:Chlorophyll / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism; D004735:Energy Transfer; D005453:Fluorescence; D005663:Furans / Q000737:chemistry; D007700:Kinetics; D008956:Models, Chemical; D015394:Molecular Structure; D011166:Porphyrins / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000737:chemistry* / Q000378:metabolism; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet; D014867:Water / Q000737:chemistry
chemical_list: D005663:Furans; D011166:Porphyrins; D014867:Water; D002734:Chlorophyll; D012710:Serum Albumin, Bovine; C018674:tetrahydrofuran; C032623:pheophorbide a