Title :
Observing interactions between the IgG antigen and anti-IgG antibody with AFM
Author :
Zhang, P.-C. ; Bai, C. ; Ho, P.K.H. ; Dai, Y. ; Wu, Y.-S.
Author_Institution :
Lab. of Biophys., Portsmouth Polytech., UK
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.
Keywords :
atomic force microscopy; biological techniques; molecular biophysics; molecular configurations; proteins; AFM; IgG antigen; McAb; anti-IgG antibody; anti-IgG monoclonal antibody; antibody molecules; antigen molecules; antigen-antibody interactions; binding numbers; binding process; binding sites; bio-macromolecular systems; complex systems; conformational changes; immunoglobulin G; spatially specific interactions; tapping-mode AFM; Atomic force microscopy; Biological materials; Electrokinetics; Humans; Immune system; Mice; Nanobioscience; Proteins; Shape; Surface morphology; Animals; Anisotropy; Antigen-Antibody Reactions; Binding Sites; Humans; Image Processing, Computer-Assisted; Immunoglobulin G; Mice; Microscopy, Atomic Force; Molecular Conformation; Molecular Weight; Surface Properties;
Journal_Title :
Engineering in Medicine and Biology Magazine, IEEE
