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.
This study describes the preparation of hydroxyapatite microspheres for local drugs delivery. The formation of the
hydroxyapatite microspheres was initiated by enzymatic decomposition of urea and accomplished by emulsification
process (water-in-oil). The microspheres obtained were sintered at 500°C. Scanning electron microscope (SEM)
indicated that the microspheres have various porous with random size, which maximizes the surface area. Cytotoxicity
was not observed after sintering. Osteoporosis drugs, alendronate and BMP-2, were loaded into HAp microspheres and
the releases of both molecules showed sustained releasing profiles.
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