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化学学报
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化学学报 ›› 2010, Vol. 68 ›› Issue (15): 1549-1552. 上一篇    

研究简报

纳米团簇-牛血清白蛋白复合物界面自组装

杨小超1,2，莫志宏*,1,2,3   

  1. (1重庆大学生物工程学院 重庆 400044)
    (2重庆大学新型微纳器件与系统技术国家重点学科实验室 重庆 400044)
    (3重庆大学化学化工学院 重庆 400044)
  • 投稿日期:2009-11-23 修回日期:2010-02-09 发布日期:2010-04-09
  • 通讯作者: 杨小超 E-mail:xcyang@cqu.edu.cn
  • 基金资助:

    科技部国际科技合作项目(批准号: 2007DFC00040)

Self-assembly of Nanocluster-Bovine Serum Albumin Conjugates at Oil/Water Interface

Yang Xiaochao1,2 Mo Zhihong*,1,2,3   

  1. (1 College of Bioengineering, Chongqing University, Chongqing 400044)
    (2 National Key Laboratory for Novel Micro/Nano Device and System Technology, Chongqing University, Chongqing 400044)
    (3 College of Chemistry & Chemical Engineering, Chongqing University, Chongqing 400044)
  • Received:2009-11-23 Revised:2010-02-09 Published:2010-04-09

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当表面电荷密度降低时, 纳米粒子-蛋白质复合物可在水包油(O/W)乳液界面自组装. 相对于纳米粒子, 粒度较小的纳米团簇(约2 nm)与蛋白质之间有更强的亲和力, 因此纳米团簇-蛋白质复合物可表现出不同的自组装特性. 为深入了解该特性, 对纳米团簇-牛血清白蛋白(BSA)在乳液界面自组装进行研究, 用Huckel方程计算自组装所需电荷密度范围, 用光学和电子显微镜研究纳米团簇与BSA的交联. 结果表明, 纳米团簇-BSA在乳液界面的自组装驱动力同样为表面电荷密度降低, 但纳米团簇与BSA的交联可造成无序自组装, 要实现有序自组装, 除需降低表面电荷密度外, 还需控制纳米团簇与BSA的结合率.

关键词: 纳米团簇, 蛋白质, 自组装, 界面

The assembly of nanoparticle-protein conjugates at oil-water interface driven by charge reduction have been established in our recent study. Comparing with nanoparticle-protein conjugates, the assembly of smaller sized nanocluster-protein conjugates would be different due to the stronger binding affinity of nanoclusters to protein than nanoparticles. To explore the assembly properties of nanocluster-protein conjugates at oil-water interface, nanoclusters were conjugated to BSA at various molar ratios. The surface charge density of the conjugates was calculated by Huckel equation, and the crosslinking between nanoclusters and bovine serum albumin (BSA) in the assembly process was investigated by microscope and transmission electron microscopy (TEM). The driven force for nanocluster-BSA interfacial assembly was determined to be charge reduction, the same as nanoparticle-protein conjuagtes. However, the crosslinking of nanocluster and BSA leading to irregular assembly was observed. To achieve regular assembly, both surface charge density and molar ratio of nanocluster and BSA have to be optimized.

Key words: nanocluster, protein, self-assembly, interface

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