| 表面活性荧光探针分子与牛血清蛋白的相互作用; Interaction of surface active fluorescence probes and bovine serum albumin | |
| 徐同宽 ; 李娜 ; 沈兴海 ; 高宏成 | |
| 2005 | |
| 关键词 | 取代3H-吲哚季铵盐 牛血清蛋白 共振能量转移 substituted 3H-indole quaternary ammonium molecule bovine serum albumin fluorescence resonance energy transfer |
| 英文摘要 | 研究了两种表面活性荧光探针分子2(对十二烷基氨基)苯基3,3二甲基5乙酯基3H吲哚基甲基二十六烷基碘化铵(1)和2(对十二烷基氨基)苯基3,3二甲基5乙酯基3H吲哚基二甲基十八烷基碘化铵(2)与牛血清蛋白(BSA)之间的相互作用。根据结合反应的温度效应求得热力学函数并推断探针分子与BSA结合的作用力类型;分子1和2与牛血清蛋白之间存在能量转移现象,根据Frster非辐射能量转移理论计算得到给体受体之间的距离分别为2.90和4.02nm。; 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 F?rster 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.; http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000232296200018&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=8e1609b174ce4e31116a60747a720701 ; SCI(E); EI; PubMed; 中文核心期刊要目总览(PKU); 中国科技核心期刊(ISTIC); 中国科学引文数据库(CSCD); 1; 09; 1443-1445; 25 |
| 语种 | 中文 |
| 出处 | 万方 ; 知网 ; SCI ; PubMed |
| 出版者 | 光谱学与光谱分析 |
| 内容类型 | 其他 |
| 源URL | [http://hdl.handle.net/20.500.11897/77929]  |
| 专题 | 化学与分子工程学院 |
| 推荐引用方式 GB/T 7714 | 徐同宽,李娜,沈兴海,等. 表面活性荧光探针分子与牛血清蛋白的相互作用, Interaction of surface active fluorescence probes and bovine serum albumin. 2005-01-01. |
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