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Affinity and Avidity

Affinity and Avidity

Hybridoma Technology

Hybridoma Technology

Hybridoma technology is used for the large-scale production of monoclonal antibodies. Monoclonal antibodies bind to only a single antigenic determinant or epitope. Such antibodies are used in research, diagnostics, and disease therapy. The hybridoma technology established in 1975 by Georges Köhler and Cesar Milstein was awarded the Nobel Prize in Medicine in 1984 for revolutionizing research and therapy.
Hybridoma Selection
Commonly used fusion techniques — electroporation,...

Antibody Structure and Classes

Antibody Structure and Classes

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.
The basic structure of an antibody consists of four protein chains: two identical heavy chains and two identical light chains. These chains are held together by disulfide bonds and other non-covalent interactions, forming a Y-shaped structure.

Cross-reactivity

Cross-reactivity

Antibody Structure

Antibody Structure

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
Antibodies consist of four polypeptide chains: two identical heavy...

Antibody Actions

Antibody Actions

Antibodies, or immunoglobulins, are critical players in the immune system's arsenal against invading pathogens. Produced by B cells and plasma cells, their primary role is to detect and bind to specific antigens, molecules found on the surface of pathogens like bacteria or viruses. Beyond antigen recognition, antibodies perform several vital functions that contribute to immune defense.
Neutralization
Antibodies can bind to pathogens, preventing them from infecting host cells. This process...

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Related Experiment Video

Updated: Dec 23, 2025

A GPC3-targeting Bispecific Antibody, GPC3-S-Fab, with Potent Cytotoxicity

A GPC3-targeting Bispecific Antibody, GPC3-S-Fab, with Potent Cytotoxicity

Published on: July 12, 2018

Multimeric antibodies with increased valency surpassing functional affinity and potency thresholds using novel

Ami Miller¹, Stephen Carr², Terry Rabbitts¹

¹Weatherall Institute of Molecular Medicine, MRC Molecular Haematology Unit, University of Oxford, John Radcliffe Hospital, Oxford, UK.

|April 23, 2020

Summary

Researchers engineered novel multivalent antibody formats called Quads to enhance therapeutic antibody potency. These Quads demonstrated increased binding and neutralization of tumor necrosis factor (TNF), offering a new therapeutic platform.

Keywords:

Multivalent antibody avidity bispecific octavalent tetravalent

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Last Updated: Dec 23, 2025

A GPC3-targeting Bispecific Antibody, GPC3-S-Fab, with Potent Cytotoxicity

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Published on: July 12, 2018

Generation of Murine Monoclonal Antibodies by Hybridoma Technology

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Published on: January 2, 2017

Construction of Synthetic Phage Displayed Fab Library with Tailored Diversity

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Published on: May 1, 2018

Area of Science:

Biotechnology
Immunology
Protein Engineering

Background:

Therapeutic antibodies are vital but have limitations in potency.
Enhancing antibody functional affinity is crucial for improved therapeutic outcomes.
Multivalent antibody formats can overcome natural affinity thresholds via avidity.

Purpose of the Study:

To introduce a novel platform of multivalent antibody formats, termed Quads.
To engineer and evaluate anti-tumor necrosis factor (TNF) Quads for enhanced potency.
To explore the versatility of Quads for generating diverse antibody formats.

Main Methods:

Utilized the self-assembling tetramerization domain from p53 to create Quads.
Engineered anti-TNF Quads and compared their binding and neutralizing capacity to parental antibodies.
Investigated the fusion of Quads with different binding domains for monospecific and bispecific formats.

Main Results:

Engineered Quads exhibited significantly increased binding potency compared to parental antibodies.
Anti-TNF Quads demonstrated enhanced neutralization of TNF-mediated cytotoxicity.
The Quad platform proved versatile for creating novel multivalent monospecific and bispecific formats.

Conclusions:

Quads represent a novel class of engineered molecules with enhanced avidity and potency.
The p53 tetramerization domain is a versatile tool for antibody engineering.
Quads offer a promising platform for developing next-generation antibody therapeutics with improved modalities.