Istituto di Fisiologia Clinica     
Preininger C., Clausen-Schaumann H., Ahluwalia A., De Rossi D. Characterization of IgG Langmuir-Blodgett films immobilized on functionalized polymers. In: Talanta, vol. 52 pp. 921 - 930. Elsevier Inc, 2000.
The bioactivity of anti-human IgG Langmuir-Blodgett (LB) films, the non-specific adsorption of protein and the topography of anti-IgG LB films have been studied for application in immunosensors. The antibody (AB) LB films were horizontally deposited on glass and functionalized polymers, such as carboxy-poly(vinyl chloride) (PVC-COOH), chloropropyl and aminopropyl sol-gel. The LB films were characterized by means of ellipsometry, atomic force microscopy (AFM) and bicinchoninic acid (BCA) protein test. The interpretation of ellipsometric data was performed using a one-layer model. Non-specifically adsorbed protein was desorbed by washing the IgG film in 0.5 M NaCl, 2 M NaCl and 1% N-cetyl-N,N,N-trimethylammoniumbromide detergent solution resulting in a 50% reduction of the film thickness. The mean thickness of an anti-IgG film on glass measured by ellipsometry, PVC-COOH and aminopropyl sol-gel was 992, 1191 and 2398 nm, respectively. According to the BCA test 6-8 mg antibody (AB) per slide was bound to the functionalized polymers, but only 3 mg AB per slide was adsorbed on glass. The average distance of anti-IgG granules as indicated by AFM measurements on PVC-COOH, chloropropyl and aminopropyl sol-gel was 42920, 3493 and 2394 nm. The average distance of granular AB structures on glass, however, was 150950 nm.
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Subject IgG

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