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Updated: Jan 5, 2026

The Bioconjugation and Radiosynthesis of 89Zr-DFO-labeled Antibodies

The Bioconjugation and Radiosynthesis of 89Zr-DFO-labeled Antibodies

Published on: February 12, 2015

Fast and Efficient Fc-Specific Photoaffinity Labeling To Produce Antibody-DNA Conjugates.

Christiane Stiller¹, Hooman Aghelpasand², Tobias Frick²

¹Department of Protein Science, School of Engineering Sciences in Chemistry, Biotechnology and Health , KTH Royal Institute of Technology, AlbaNova University Center , 106 91 Stockholm , Sweden.

Bioconjugate Chemistry

|October 15, 2019

Summary

This summary is machine-generated.

Researchers developed a straightforward method for creating high-quality antibody-DNA conjugates, essential for advanced protein analysis. This technique ensures consistent results and enables efficient screening of these valuable tools.

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Area of Science:

Bioconjugation Chemistry
Molecular Biology
Protein Analysis

Background:

Antibody-DNA conjugates are crucial for DNA-assisted protein analysis, but their production requires efficient and high-quality methods.
Existing methods for producing antibody-DNA conjugates can be complex and may suffer from batch-to-batch variability.

Purpose of the Study:

To develop an easy, fast, and reliable synthesis route for covalent antibody-DNA conjugates with a defined conjugation site.
To demonstrate the functionality of these conjugates in protein detection and quantification assays.

Main Methods:

Utilized the Z domain of protein A with unnatural amino acid 4-benzoylphenylalanine (BPA) for photoaffinity labeling of the antibody Fc region.
Employed Sortase A enzymatic coupling to attach DNA-oligonucleotides (triple-glycine modified) to the Z(xBPA) domains.
Validated the method on commonly used IgG antibodies.

Main Results:

Successfully produced covalent antibody-DNA conjugates with a defined conjugation site and low batch-to-batch variability.
Demonstrated retained functionality of both antibody and DNA components in antibody-antigen binding detection.
Showcased the utility of Droplet Barcode Sequencing for Protein analysis (DBS-Pro) in quantifying protein abundances.

Conclusions:

The developed modular approach provides a convenient strategy for producing high-quality antibody-DNA conjugates.
The method ensures consistent conjugate production and retains the functionality of both antibody and DNA components.
The approach facilitates efficient screening of various antibody-DNA conjugates for diverse protein analysis applications.