title: [Study on the interaction between ICT fluorescence probe and bovine serum albumins].
abstract: The present article studied the interaction between intramolecular charge transfer fluorescence probe-1-keto-2-(p-dimethylaminobenzal)-tetrohydronaphthalene (KDTN) and bovine serum albumins (BSA). With the concentration of KDTN increasing, the fluorescence of BSA rapidly quenched and the fluorescence peak gradually blue-shifted. The result indicated that they were bound mainly by hydrophobic interaction. The binding sites is 0.94 (3 degrees C) and the equilibrium constant K is 3.27 x 10(4) L x mol(-1). Temperature increment is advantageous to the combination. It is a single static quenching process that the fluorescence of BSA quenches, which is induced by the combination of KDTN and BSA. Further study showed that different substances had different effects on the combination of KDTN and BSA.
authors.affiliation: Department of Chemistry, Shanxi University, Taiyuan 030006, China. sxyclyf@sina.com
authors.forename: Yu-Fang
authors.initials: YF
authors.lastname: Liu
authors.forename: Jian-Qing
authors.initials: JQ
authors.lastname: Li
authors.forename: Zhi-Cheng
authors.initials: ZC
authors.lastname: Xu
authors.forename: Yan-Li
authors.initials: YL
authors.lastname: Wei
authors.forename: Shao-Min
authors.initials: SM
authors.lastname: Shuang
authors.forename: Chuan
authors.initials: C
authors.lastname: Dong
mesh_terms: D000818:Animals; D002417:Cattle; D015394:Molecular Structure; D009281:Naphthalenes / Q000032:analysis* / Q000737:chemistry; D012710:Serum Albumin, Bovine / Q000032:analysis* / Q000737:chemistry; D013050:Spectrometry, Fluorescence / Q000379:methods*; D013696:Temperature
chemical_list: C550744:1-keto-2-(p-dimethylaminobenzal)tetrohydronaphthalene; D009281:Naphthalenes; D012710:Serum Albumin, Bovine