期刊
BIOCONJUGATE CHEMISTRY
卷 30, 期 11, 页码 2790-2798出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.bioconjchem.9b00548
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资金
- Erling Persson Family Foundation
- Swedish Research Council (VR) [2018-06228]
- Swedish Research Council [2018-06228] Funding Source: Swedish Research Council
Antibody DNA conjugates are powerful tools for DNA-assisted protein analysis. Growing usage of these methods demands efficient production of high-quality conjugates. We developed an easy and fast synthesis route yielding covalent antibody-DNA conjugates with a defined conjugation site and low batch-to-batch variability. We utilize the Z domain from protein A, containing the unnatural amino acid 4-benzoylphenylalanine (BPA) for photoaffinity labeling of the antibodies' Fc region. Z(xBPA) domains are C-terminally modified with triple-glycine (G(3))-modified DNA-oligonucleotides enzymatic Sortase A coupling. We reliable modification of the most commonly used IgG's. To prove our conjugates' functionality, we detected antibody-antigen binding events in an assay called Droplet Barcode Sequencing for Protein analysis (DBS-Pro). It confirms not only retained functionality for both conjugate parts but also the potential of using DBS-Pro for quantifying protein abundances. As intermediates are easily storable and our approach is modular, it offers a convenient strategy for screening various antibody-DNA conjugates using the same starting material.
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