Abstract
An antibody can be specifically oxidized with periodate (NaIO4) on the carbohydrate side chains at its C-terminal. Rabbit anti-hepatitis B surface antigen (anti-HBsAg) IgG antibodies were bound to the silicon wafer surface by covalent bonds between aldehydes generated on the carbohydrate side chains of the antibodies and the reactive amine groups of 3-aminopropyltriethoxylsilane(APTES)-modified silicon wafer surfaces. A control experiment was also performed by direct attachment of antibodies to glutaraldehyde-treated silicon surfaces. Two different coupling antibody strategies were investigated in this paper. Atomic force microscopy was used to observe the orientation of the site-directed and random attachment of rabbit anti-HBsAg IgG antibodies and the conservation of their antigen-binding capacity (AgBC) was assessed using an enzyme immunoassay (EIA).
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Weiping, Q., Bin, X., Lei, W. et al. Orientation of Antibodies on a 3-Aminopropyltriethoxylsilane-Modified Silicon Wafer Surface. Journal of Inclusion Phenomena 35, 419–429 (1999). https://doi.org/10.1023/A:1008192209162
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DOI: https://doi.org/10.1023/A:1008192209162