Preparation of surface imprinted core-shell particles via a metal chelating strategy: specific recognition of porcine serum albumin

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• 作者：Qinran Li ; Kaiguang Yang ; Senwu Li ; Lukuan Liu ; Lihua Zhang…
• 关键词：Molecular imprinting ; Metal ion immobilization ; Protein imprinting ; Silica particles ; HPLC ; Transmission electron microscopy
• 刊名：Microchimica Acta
• 出版年：2016
• 出版时间：January 2016
• 年：2016
• 卷：183
• 期：1
• 页码：345-352
• 全文大小：1,440 KB
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• 作者单位：Qinran Li (1) (2)
  Kaiguang Yang (1)
  Senwu Li (1) (2)
  Lukuan Liu (1) (2)
  Lihua Zhang (1)
  Zhen Liang (1)
  Yukui Zhang (1)
  
  1. Key Laboratory of Separation Science for Analytical Chemistry, National Chromatographic R.&.A Center, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, 116023, China
  2. University of Chinese Academy of Sciences, Beijing, 100039, China
  
• 刊物类别：Chemistry and Materials Science
• 刊物主题：Chemistry
  Analytical Chemistry
  Inorganic Chemistry
  Physical Chemistry
  Characterization and Evaluation Materials
  Monitoring, Environmental Analysis and Environmental Ecotoxicology
  
• 出版者：Springer Wien
• ISSN：1436-5073

文摘

We describe the synthesis of molecularly imprinted core-shell microparticles via a metal chelating strategy that assists in the creation of selective recognition sites for albumin. Porcine serum albumin (PSA) was immobilized on silica beads via copper(II) chelation interaction. A solution containing 2-hydroxyethyl methacrylate and methacrylic acid as the monomers was mixed with the above particles, and free radical polymerization was performed at 25 °C. Copper ion and template were then removed to obtain PSA-imprinted core-shell particles (MIPs) with a typical diameter of 5 μm. The binding capacity of such MIP was 8.9 mg protein per gram of MIPs, and the adsorption equilibrium was established within <20 min. The imprinting factor for PSA reached 2.6 when the binding capacity was 7.7 mg protein per gram of MIPs. The use of such MIPs enabled PSA to be selectively recognized even in presence of the competitive proteins ribonuclease B, cytochrome c, and myoglobin. The results indicate that this imprinting strategy for protein may become a promising method to prepare MIPs for protein recognition.