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Binding affinities/avidities of antibody–antigen interactions: Quantification and scale-up implications by Huading Zhang; P. Stephen Williams; Maciej Zborowski; Jeffrey J. Chalmers is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract Bioaffinity interactions have been, and continue to be, successfully adapted from nature for use in separation and detection applications. It has been previously reported that the magnetophoretic mobility of labeled cells show a saturation type phenomenon as a function of the concentration of the free antibody–magnetic nanoparticle conjugate which is consistent with other reports of antibody–fluorophore binding. Starting with the standard antibody–antigen relationship, a model was developed which takes into consideration multi‐valence interactions, and various attributes of flow cytometry (FCM) and cell tracking velocimetry (CTV) measurements to determine both the apparent dissociation constant and the antibody‐binding capacity (ABC) of a cell. This model was then evaluated on peripheral blood lymphocytes (PBLs) labeled with anti CD3 antibodies conjugated to FITC, PE, or DM (magnetic nanoparticles). Reasonable agreements between the model and the experiments were obtained. In addition, estimates of the limitation of the number of magnetic nanoparticles that can bind to a cell as a result of steric hinderance was consistent with measured values of magnetophoretic mobilit

Who reads Binding affinities/avidities of antibody–antigen interactions: Quantification and scale-up implications?

Author

Huading Zhang; P. Stephen Williams; Maciej Zborowski; Jeffrey J. Chalmers

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); Wiley - V C H Verlag GmbbH & Co.; Wiley (ISSN 0006-3592)

Published

2006

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)