Abstract

Spatially specific interactions between the immunoglobulin G (IgG) antigen and anti-IgG monoclonal antibody (McAb) have been studied in detail by tapping-mode AFM. The binding numbers and binding sites of the antigen molecules with antibody molecules, as well as the conformational changes during the binding process have been revealed. The wider application of this technique to complex systems has considerable potential for study of a variety of antigen-antibody interactions and may be extended to other bio-macromolecular systems.

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