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

Volume

16

Issue

2

fYear

1997

Firstpage

42

Lastpage

46

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;

fLanguage

English

Journal_Title

Engineering in Medicine and Biology Magazine, IEEE

Publisher

ieee

ISSN

0739-5175

Type

jour

DOI

10.1109/51.582175

Filename

582175