title: [Interaction of surface active fluorescence probes and bovine serum albumin].
abstract: The binding between two surface-active substituted 3H-indole fluorescence probes, i. e., iodo-dihexadecyl methyl-2-(p-dodecyl amino phenyl)-3, 3-dimethyl-5-carboethoxy-3H-indole ammonium and iodo-dimethyloctadecyl-2-(p-dodecyl amino phenyl)-3,3-dimethyl-5-carboethoxy-3H-indole ammonium, and bovine serum albumin (BSA) in aqueous solution was studied using fluorescence. The binding constant and binding site number of molecule 1 and molecule 2 with BSA were obtained. It was confirmed that electrostatic interaction is the primary driving force for the combination of BSA with molecule 1 or molecule 2. According to the Förster resonance energy transfer theory, the distances between molecule 1, molecule 2 and tryptophan of BSA were calculated to be 2.90 nm and 4.02 nm, respectively.
authors.affiliation: Department of Applied Chemistry, College of Chemistry and Molecular Engineering, Peking University, Beijing 100871, China.
authors.forename: Tong-kuan
authors.initials: TK
authors.lastname: Xu
authors.forename: Na
authors.initials: N
authors.lastname: Li
authors.forename: Xing-hai
authors.initials: XH
authors.lastname: Shen
authors.forename: Hong-cheng
authors.initials: HC
authors.lastname: Gao
mesh_terms: D000465:Algorithms; D000818:Animals; D002417:Cattle; D005456:Fluorescent Dyes / Q000737:chemistry* / Q000378:metabolism; D007211:Indoles / Q000737:chemistry / Q000378:metabolism; D007700:Kinetics; D015394:Molecular Structure; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000737:chemistry* / Q000378:metabolism; D013050:Spectrometry, Fluorescence; D055672:Static Electricity
chemical_list: D005456:Fluorescent Dyes; D007211:Indoles; C550014:iodo-dihexadecylmethyl-2-(p-dodecylaminophenyl)-3,3-dimethyl-5-carboethoxy-3H-indole ammonium; C550015:iodo-dimethyloctadecyl-2-(p-dodecylaminophenyl)-3,3-dimethyl-5-carboethoxy-3H-indole ammonium; D012710:Serum Albumin, Bovine