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Related Concept Videos

The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

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The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:
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Antibody Structure01:10

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Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
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Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
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Antibody Structure and Classes01:25

Antibody Structure and Classes

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Antibodies, also known as immunoglobulins, are produced by B cells in response to foreign substances, such as bacteria and viruses. These proteins are critical for recognizing and neutralizing these substances, protecting the body from potential harm.
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Related Experiment Video

Updated: Apr 28, 2026

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
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Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

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Highly parallel characterization of IgG Fc binding interactions.

Austin W Boesch1, Eric P Brown1, Hao D Cheng2

  • 1Thayer School of Engineering, Dartmouth College, Hanover, NH USA.

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|June 14, 2014
PubMed
Summary

A new microsphere assay rapidly assesses antibody binding to receptors, aiding antibody therapeutics development and understanding immune responses. This method offers a faster alternative to traditional biophysical techniques for antibody characterization.

Keywords:
Fc domainFcγ receptorIgGantibodyglycosylationlectinluminexmultiplex

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Area of Science:

  • Immunology
  • Biotechnology
  • Biochemistry

Background:

  • The antibody constant (Fc) domain's interaction with innate immune cells and complement is crucial for in vivo antibody function.
  • Assessing these binding interactions is vital for developing improved antibody therapies and understanding immune responses in infection, vaccination, and autoimmune diseases.

Purpose of the Study:

  • To develop a rapid, highly parallel assay for assessing antibody binding to various Fc receptors and lectins.
  • To provide a valuable tool for characterizing monoclonal antibodies, clinical samples, and Fc receptor binding preferences.

Main Methods:

  • Conjugation of Fc and glycan binding proteins (e.g., FcγR, lectins) to coded microspheres.
  • Quantification of antibody interactions with these immobilized receptors using a microsphere-based assay.
  • Assessment of binding preferences and affinities across different antibody formats and variants.

Main Results:

  • Demonstrated the assay's capability for both qualitative and quantitative assessment of antibody-receptor interactions.
  • Successfully characterized binding across various IgG subclasses, Fc domain point mutants, and antibodies with differing glycosylation patterns.
  • Validated the assay as a rapid proxy for slower, more resource-intensive biophysical methods.

Conclusions:

  • The developed microsphere assay offers a fast and efficient method for evaluating antibody-Fc receptor interactions.
  • This assay facilitates the characterization of antibody therapeutics, clinical samples, and candidate Fc receptors.
  • Provides a valuable tool for advancing antibody engineering and understanding immune-mediated processes.