Interaction of Surface-active Fluorescence Probes with Bovine Serum Albumin  

作　　者：TongKuanXU XingHalSHEN NaLI HongChengGAO 

机构地区：[1]CollegeofChemistryEngineeringandMaterials,DalianInstituteofLightIndustry,Dalian116034／／CollegeofChemistryandMolecularEngineering,PekingUniversity,Beijing100871 [2]CollegeofChemistryandMolecularEngineering,PekingUniversity,Beijing100871

出　　处：《Chinese Chemical Letters》2005年第7期943-946,共4页中国化学快报（英文版）

基　　金：The work was supported by the National Natural Science Foundation of China(Grant No.90206020,29901001).

摘　　要：The binding between three surface-active substituted 3H-indole fluorescence probes and bovine serum albumin (BSA) in aqueous solution was studied using fluorescence quenching. The binding constants of 3H-indole molecules with BSA were obtained. According to the F?rster resonance energy transfer theory, the distances between 3H-indole molecules and tryptophan of BSA were calculated. The results show that the oligoethyloxyethylene chain of 3H-indole molecules is longer, the binding between them is stronger, the energy transfer efficiency is higher, and the distance between tryptophan and 3H-indole is nearer.

关 键 词：Substituted 3H-indole quaternary ammonium molecule bovine serum albumin fluorescence resonance energy transfer. 

分 类 号：Q512.1[生物学—生物化学]