4.8 Article

Nanocapsules incorporating IgG Fc-binding domain derived from Staphylococcus aureus protein A for displaying IgGs on immunosensor chips

期刊

BIOMATERIALS
卷 32, 期 6, 页码 1455-1464

出版社

ELSEVIER SCI LTD
DOI: 10.1016/j.biomaterials.2010.10.057

关键词

Biosensor; Gold; Nanoparticle; Scaffold; Self assembly; Surface modification

资金

  1. Bio-oriented Technology Research Advancement Institution (BRAIN) of Japan
  2. Program for Promotion of Basic and Applied Researches for Innovations in Bio-oriented Industry (BRAIN)
  3. Japan Science and Technology Agency (JST)
  4. Ministry of Health & Welfare, Republic of Korea [A062254]
  5. Korea Science and Engineering Foundation [2008-03876]
  6. National Research Foundation of Korea [2008-03876] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
  7. Grants-in-Aid for Scientific Research [23710143, 22650111] Funding Source: KAKEN

向作者/读者索取更多资源

To enhance the sensitivities and antigen-binding capacities of immunosensors, oriented immobilization of antibodies on the surface of the sensor chip is critical, but to date, this has not been adequately achieved. We describe a way of adsorbing immunoglobulin (Ig) proteins onto 32-nm bio-nanocapsules (BNCs) through IgG Fc-binding domains derived from Staphylococcus aureus protein A (ZZ-BNC). This arrangement permits similar to 60 molecules of mouse total IgG bind to ZZ-BNC and all the IgG Fv regions to be displayed outwardly for the effective binding of antigens. ZZ-BNCs adsorbed onto the gold surface of the sensor chip of the quartz crystal microbalance (QCM) could markedly enhance the sensitivity and antigen-binding capacity of the chip. On the sensor chip of surface plasmon resonance (SPR), antibodies on the ZZ-BNCs showed higher affinities to each antigen than those on protein A. The BNC-coated sensor chip is very stable, and should prove useful for various immunosensor applications due to oriented immobilization of antibodies. (C) 2010 Elsevier Ltd. All rights reserved.

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