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

Biomaterials. 2011 Feb;32(6):1455-64. doi: 10.1016/j.biomaterials.2010.10.057. Epub 2010 Nov 23.

Abstract

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 approximately 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Biosensing Techniques / methods*
  • Goats
  • Humans
  • Immunoglobulin Fc Fragments / chemistry*
  • Immunoglobulin G / chemistry*
  • Mice
  • Microscopy, Atomic Force
  • Microscopy, Electron, Transmission
  • Nanocapsules / chemistry*
  • Nanocapsules / ultrastructure
  • Nanotechnology
  • Rabbits
  • Rats
  • Sheep
  • Staphylococcal Protein A / chemistry*
  • Surface Plasmon Resonance

Substances

  • Immunoglobulin Fc Fragments
  • Immunoglobulin G
  • Nanocapsules
  • Staphylococcal Protein A