Diagnostic assays based on antibodies rest on their adsorption, usually on hydrophobic substrates, in an orientation allowing interactions between variable domains and corresponding antigens. The present work is part of a project which aims at producing chimeric antibodies showing a preferred adsorption in end-on orientation, with the constant domain interacting with the substrate. The ability of different isotypes of rat and mouse immuno-?-globulins to adsorb and to recognize the corresponding antigen was examined using quartz crystal microbalance. Results show that the highest adsorbed amount is obtained with IgG2a from mouse, while IgG1 and IgG2a from rat achieve the highest level of antigen binding. For most antibodies, the molar ratio of bound antigen vs adsorbed antibodies was in the range of 0.6-0.9, indicating a preferred end-on adsorption, in contradiction with the fact that side-on adsorption is energetically more favorable. Random sequential adsorption modeling was then successfully used to understand this paradox.

Orientation of adsorbed antibodies:<i> </i>In situ monitoring by QCM and random sequential adsorption modeling

243rd National Meeting (2012)

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Orientation of adsorbed antibodies: In situ monitoring by QCM and random sequential adsorption modeling