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Diversity of Antigen Receptors

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Related Experiment Video

Updated: Jul 26, 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

Sequence-defined antibody-recruiting macromolecules.

Resat Aksakal¹, Corentin Tonneaux², Annemiek Uvyn³

¹Polymer Chemistry Research Group, Centre of Macromolecular Chemistry (CMaC), Department of Organic and Macromolecular Chemistry, Faculty of Sciences, Ghent University 9000 Ghent Belgium nezha.badi@ugent.be filip.duprez@ugent.be.

Chemical Science

|June 23, 2023

Summary

This summary is machine-generated.

Novel antibody-recruiting molecules utilize sequence-defined macromolecules to enhance therapeutic agent design. These molecules show increased binding avidity, offering insights for developing new antibody-recruiting therapies.

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Area of Science:

Biotechnology
Immunology
Materials Science

Background:

Antibody-recruiting molecules (ARMs) are a novel therapeutic class that harness the immune system to eliminate target cells.
Macromolecular scaffolds with multiple antibody-binding ligands offer superior avidity compared to single-ligand systems.

Purpose of the Study:

To synthesize sequence-defined macromolecules for antibody recruitment.
To investigate the impact of ligand spacing on antibody binding avidity.
To explore structure-activity relationships for designing novel ARMs.

Main Methods:

Synthesis of sequence-defined oligomers using solid-phase thiolactone chemistry.
Incorporation of dinitrophenol (DNP) as a model antibody-recruiting motif.
Biolayer interferometry and molecular modeling for binding analysis and structural insights.

Main Results:

Oligomers with adjacent DNP motifs demonstrated significantly enhanced avidity for anti-DNP antibodies.
Varying DNP motif spacing on the macromolecular backbone influenced binding interactions.
Molecular modeling elucidated ligand accessibility and macromolecular dynamics.

Conclusions:

Sequence-defined macromolecules provide a powerful platform for studying structure-activity relationships in ARMs.
Optimized ligand presentation on macromolecular scaffolds can enhance antibody recruitment efficacy.
Findings offer valuable insights for the rational design of next-generation antibody-recruiting therapeutics.