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Proceedings Paper

Highly efficient antibody immobilization with multimeric protein Gs coupled magnetic silica nanoparticles
Author(s): J. H. Lee; H. K. Choi; J. H. Chang
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Paper 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.

Paper Details

Date Published: 12 September 2011
PDF: 8 pages
Proc. SPIE 8099, Biosensing and Nanomedicine IV, 80990L (12 September 2011); doi: 10.1117/12.893366
Show Author Affiliations
J. H. Lee, Korea Institute of Ceramic Engineering and Technology (Korea, Republic of)
H. K. Choi, Korea Institute of Ceramic Engineering and Technology (Korea, Republic of)
J. H. Chang, Korea Institute of Ceramic Engineering and Technology (Korea, Republic of)


Published in SPIE Proceedings Vol. 8099:
Biosensing and Nanomedicine IV
Hooman Mohseni; Massoud H. Agahi; Manijeh Razeghi, Editor(s)

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