Highly efficient antibody immobilization with multimeric protein Gs coupled magnetic silica nanoparticles

J. H. Lee; H. K. Choi; J. H. Chang

doi:10.1117/12.893366

12 September 2011 Highly efficient antibody immobilization with multimeric protein Gs coupled magnetic silica nanoparticles

J. H. Lee, H. K. Choi, J. H. Chang

Author Affiliations +

Proceedings Volume 8099, Biosensing and Nanomedicine IV; 80990L (2011) https://doi.org/10.1117/12.893366
Event: SPIE NanoScience + Engineering, 2011, San Diego, California, United States

Abstract

This work reports the immobilization of monomeric, dimeric and trimer protein Gs onto silica magnetic nanoparticles for self-oriented antibody immobilization. To achieve this, we initially prepared the silica-coated magnetic nanoparticle having about 170 nm diameters. The surface of the silica coated magnetic nanoparticles was modified with 3- aminopropyl-trimethoxysilane (APTMS) to chemically link to multimeric protein Gs. The conjugation of amino groups on the SiO2-MNPs to cysteine tagged in multimeric protein Gs was performed using a sulfo-SMCC coupling procedure. The binding efficiencies of monomer, dimer and trimer were 77 %, 67 % and 55 % respectively. However, the efficiencies of antibody immobilization were 70 %, 83 % and 95 % for monomeric, dimeric and trimeric protein G, respectively. To prove the enhancement of accessibility by using multimeric protein G, FITC labeled goat-anti-mouse IgG was treated to mouse IgG immobilized magnetic silica nanoparticles through multimeric protein G. FITC labeled goat anti-mouse IgGs were more easily bound to mouse IgG immobilized by trimeric protein G than others. Finally protein G bound silica magnetic nanoparticles were utilized to develop highly sensitive immunoassay to detect hepatitis B antigen.

Citation Download Citation

J. H. Lee, H. K. Choi, and J. H. Chang "Highly efficient antibody immobilization with multimeric protein Gs coupled magnetic silica nanoparticles", Proc. SPIE 8099, Biosensing and Nanomedicine IV, 80990L (12 September 2011); https://doi.org/10.1117/12.893366

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