Acta Chimica Sinica ›› 2010, Vol. 68 ›› Issue (17): 1741-1748. Previous Articles     Next Articles

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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)
  • 收稿日期:2009-09-14 修回日期:2010-01-13 出版日期:2010-09-14 发布日期:2010-04-29
  • 通讯作者: 何华

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 Online:2010-09-14 Published:2010-04-29

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