化学学报 ›› 2010, Vol. 68 ›› Issue (17): 1741-1748. 上一篇    下一篇

研究论文

不同代PAMAM树状大分子与牛血清白蛋白的相互作用研究

张怀敬1,何华*,1,2,李杉杉1,芦金荣3,Chuong, Pham-Huy4   

  1. (1中国药科大学分析化学教研室 南京 210009)
    (2药物质量与安全预警教育部重点实验室 南京 210009)
    (3中国药科大学有机化学教研室 南京 210009)
    (4 Faculty of Pharmacy, University of Paris V, 4 avenue de l Observatoire, 75006)
  • 投稿日期:2009-09-14 修回日期:2010-01-13 发布日期:2010-04-29
  • 通讯作者: 何华 E-mail:dochehua@163.com

Study on the Interactions of Different PAMAM Dendrimers with Bovine Serum Albumin

Zhang Huaijing1 He Hua*,1,2 Li Shanshan1 Lu Jinrong3 Chuong Pham-Huy4   

  1. (1 Division of Analytical Chemistry, China Pharmaceutical University, Nanjing 210009)
    (2 Key Laboratory of Drug Quality Control and Pharmacovigilance (China Pharmaceutical University), Ministry of Education)
    (3 Division of Organic Chemistry, China Pharmaceutical University, Nanjing 210009)
    (4 Faculty of Pharmacy, University of Paris V, 4 avenue de l Observatoire, 75006 Paris, France)
  • Received:2009-09-14 Revised:2010-01-13 Published:2010-04-29

采用发散法合成了以乙二胺为核的聚酰胺-胺型(PAMAM)树状大分子, 并应用荧光光谱法研究了生理条件下(pH=7.4) 3.0代(G3.0)、3.5代(G3.5)和4.0代(G4.0)PAMAM树状大分子与牛血清白蛋白(BSA)的相互作用. 结果表明, 三种PAMAM树状大分子都能引起牛血清白蛋白荧光猝灭, 其程度主要取决于各自末端基团的性质, 猝灭机制属于静态猝灭. G4.0 PAMAM, G3.5 PAMAM和G3.0 PAMAM与BSA的猝灭常数分别为2.73, 1.69, 1.55 L•mmol-1. 同时考察了体系pH值及离子强度的变化对PAMAM与BSA相互作用的影响. 此外, 同步荧光和紫外光谱法(UV)以及红边激发荧光位移(REES)等方法的研究结果表明, PAMAM树状大分子的存在改变了BSA的构象.

关键词: PAMAM树状大分子, 牛血清白蛋白, 荧光猝灭, 同步荧光光谱, 红边激发荧光位移

Polyamidoamine (PAMAM) dendrimers have been synthesized by divergent with ethylenediamine as core. The interaction between PAMAM including amine-terminated generation 4.0 (G4.0)、generation 3.0 (G3.0) PAMAM and ester-terminated generation 3.5 (G3.5) PAMAM dendrimers and bovine serum albumin (BSA) under physiological condition was studied by fluorescence spectroscopy. The results showed that the fluorescence intensity of BSA decreased with the addition of different PAMAM dendrimers, the quenching extent strongly depends on the type and amounts of their surface groups. The quenching mechanism was static quenching mechanism. The quenching constants of G4.0 PAMAM, G3.5 PAMAM, G3.0 PAMAM with BSA were 2.73, 1.69, 1.55 L•mmol-1, respectively. The influence of pH and ionic strength on the interactions was also investigated. Furthermore, synchronous fluorescence, ultraviolet-visible spectra analysis (UV), and red edge excitation shift (REES) showed that PAMAM dendrimers could change the conformation of BSA.

Key words: PAMAM dendrimers, bovine serum albumin, fluorescence quenching, synchronous fluorescence, red edge excitation shift