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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...

Affinity and Avidity

Affinity and Avidity

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Related Experiment Video

Updated: May 21, 2025

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Published on: January 14, 2020

CDRxAbs: antibody small-molecule conjugates with computationally designed target-binding synergy.

Jingzhou Wang^1,2,3, Aiden J Aceves^1,4, Nicholas J Friesenhahn²

¹Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125, United States.

Protein Engineering, Design & Selection : PEDS

|March 21, 2025

Summary

This summary is machine-generated.

We developed CDR-extended antibodies (CDRxAbs), a novel class of molecular agents. These bioconjugates enhance small molecule binding affinity and specificity to targets.

Keywords:

Antibody Drug Conjugate Antibody Engineering CDRxAb Computational Design Protein Design

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Area of Science:

Bioconjugation chemistry
Computational protein design
Molecular recognition

Background:

Bioconjugates offer refined therapeutic action by combining molecular advantages.
Current limitations exist in optimizing small molecule therapeutics for binding affinity and specificity.

Purpose of the Study:

To introduce CDR-extended antibodies (CDRxAbs) as a new class of molecular recognition agents.
To demonstrate the ability of CDRxAbs to improve small molecule binding affinity and specificity.

Main Methods:

Utilized computational protein design with full atomic simulation.
Integrated small molecules into antibody binding interfaces.
Designed and optimized nanobody-biotin conjugates for proof-of-concept.

Main Results:

Achieved >20-fold affinity improvement for nanobody-biotin conjugates against protein targets.
Demonstrated step-wise optimization of binding kinetics and protein stability.
Validated the CDRxAb concept in a proof-of-concept study.

Conclusions:

CDRxAbs represent a novel approach to enhance small molecule-based therapeutics.
This methodology promises to expand the chemical and target space for molecular recognition agents.
CDRxAbs offer improved binding affinity and specificity compared to small molecules alone.